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Database: PDB
Entry: 1Z7E
LinkDB: 1Z7E
Original site: 1Z7E 
HEADER    HYDROLASE                               24-MAR-05   1Z7E              
TITLE     CRYSTAL STRUCTURE OF FULL LENGTH ARNA                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN ARNA;                                              
COMPND   3 CHAIN: A, B, C, D, E, F;                                             
COMPND   4 SYNONYM: HYPOTHETICAL PROTEIN YFBG;                                  
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 OTHER_DETAILS: FULL LENGTH                                           
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 GENE: PMRI, YFBG;                                                    
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: ROSETTA (DE3);                             
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PMS122;                                   
SOURCE  10 OTHER_DETAILS: PLASMID IS AN ENGINEERED VARIANT OF THE               
SOURCE  11 PET28                                                                
KEYWDS    ROSSMANN FOLD; OB-LIKE FOLD, HYDROLASE                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.Z.GATZEVA-TOPALOVA,A.P.MAY,M.C.SOUSA                                
REVDAT   3   24-FEB-09 1Z7E    1       VERSN                                    
REVDAT   2   21-JUN-05 1Z7E    1       JRNL                                     
REVDAT   1   07-JUN-05 1Z7E    0                                                
JRNL        AUTH   P.Z.GATZEVA-TOPALOVA,A.P.MAY,M.C.SOUSA                       
JRNL        TITL   STRUCTURE AND MECHANISM OF ARNA: CONFORMATIONAL              
JRNL        TITL 2 CHANGE IMPLIES ORDERED DEHYDROGENASE MECHANISM IN            
JRNL        TITL 3 KEY ENZYME FOR POLYMYXIN RESISTANCE                          
JRNL        REF    STRUCTURE                     V.  13   929 2005              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   15939024                                                     
JRNL        DOI    10.1016/J.STR.2005.03.018                                    
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 135954.500                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 95.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 126417                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.225                           
REMARK   3   FREE R VALUE                     : 0.247                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 12667                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.002                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.11                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 89.80                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 10626                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3170                       
REMARK   3   BIN FREE R VALUE                    : 0.3340                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 9.90                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 1169                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.010                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 30148                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 408                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 44.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.02000                                             
REMARK   3    B22 (A**2) : -12.76000                                            
REMARK   3    B33 (A**2) : 14.78000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.37                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.48                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.42                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.54                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.40                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.80                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.91                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 0.970 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.690 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.610 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.630 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.39                                                 
REMARK   3   BSOL        : 33.73                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : ATP_UGA_REV.PARAM                              
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : ATP_UGA_REV.TOP                                
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1Z7E COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-APR-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB032391.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-DEC-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1808                             
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL, SI(111)            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 131520                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 1.300                              
REMARK 200  R MERGE                    (I) : 0.07900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.34900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: 1U9J, 1YRW                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 67.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.70                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES PH 7.0, 10% ETHYLENE            
REMARK 280  GLYCOL, 9% PEG 8000, 14 MM 2MERCAPTOETHANOL AND 10 MM ATP;          
REMARK 280  PROTEIN WAS PRE-INCUBATED ON ICE WITH 3MM UDP-GLCA AND 3 MM         
REMARK 280  MGSO4 , VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 289K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       75.84450            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      130.99600            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       83.11350            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      130.99600            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       75.84450            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       83.11350            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 33970 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 145130 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -146.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F                      
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ASN A    35                                                      
REMARK 465     PRO A    36                                                      
REMARK 465     GLY A    37                                                      
REMARK 465     GLU A    38                                                      
REMARK 465     LYS A    39                                                      
REMARK 465     ALA A    40                                                      
REMARK 465     PHE A    41                                                      
REMARK 465     TYR A    42                                                      
REMARK 465     ASN A   305                                                      
REMARK 465     SER A   306                                                      
REMARK 465     GLN A   307                                                      
REMARK 465     PRO A   308                                                      
REMARK 465     ALA A   309                                                      
REMARK 465     CYS A   310                                                      
REMARK 465     THR A   311                                                      
REMARK 465     ALA A   312                                                      
REMARK 465     ARG A   313                                                      
REMARK 465     ASP A   657                                                      
REMARK 465     LYS A   658                                                      
REMARK 465     PRO A   659                                                      
REMARK 465     SER A   660                                                      
REMARK 465     ASN B    35                                                      
REMARK 465     PRO B    36                                                      
REMARK 465     GLY B    37                                                      
REMARK 465     GLU B    38                                                      
REMARK 465     LYS B    39                                                      
REMARK 465     ALA B    40                                                      
REMARK 465     PHE B    41                                                      
REMARK 465     TYR B    42                                                      
REMARK 465     ASN B   305                                                      
REMARK 465     SER B   306                                                      
REMARK 465     GLN B   307                                                      
REMARK 465     PRO B   308                                                      
REMARK 465     ALA B   309                                                      
REMARK 465     CYS B   310                                                      
REMARK 465     THR B   311                                                      
REMARK 465     ALA B   312                                                      
REMARK 465     ARG B   313                                                      
REMARK 465     ASP B   657                                                      
REMARK 465     LYS B   658                                                      
REMARK 465     PRO B   659                                                      
REMARK 465     SER B   660                                                      
REMARK 465     ASN C    35                                                      
REMARK 465     PRO C    36                                                      
REMARK 465     GLY C    37                                                      
REMARK 465     GLU C    38                                                      
REMARK 465     LYS C    39                                                      
REMARK 465     ALA C    40                                                      
REMARK 465     PHE C    41                                                      
REMARK 465     TYR C    42                                                      
REMARK 465     ASN C   305                                                      
REMARK 465     SER C   306                                                      
REMARK 465     GLN C   307                                                      
REMARK 465     PRO C   308                                                      
REMARK 465     ALA C   309                                                      
REMARK 465     CYS C   310                                                      
REMARK 465     THR C   311                                                      
REMARK 465     ALA C   312                                                      
REMARK 465     ARG C   313                                                      
REMARK 465     ASP C   657                                                      
REMARK 465     LYS C   658                                                      
REMARK 465     PRO C   659                                                      
REMARK 465     SER C   660                                                      
REMARK 465     ASN D    35                                                      
REMARK 465     PRO D    36                                                      
REMARK 465     GLY D    37                                                      
REMARK 465     GLU D    38                                                      
REMARK 465     LYS D    39                                                      
REMARK 465     ALA D    40                                                      
REMARK 465     PHE D    41                                                      
REMARK 465     TYR D    42                                                      
REMARK 465     ALA D   309                                                      
REMARK 465     CYS D   310                                                      
REMARK 465     THR D   311                                                      
REMARK 465     ALA D   312                                                      
REMARK 465     ASP D   657                                                      
REMARK 465     LYS D   658                                                      
REMARK 465     PRO D   659                                                      
REMARK 465     SER D   660                                                      
REMARK 465     ASN E    35                                                      
REMARK 465     PRO E    36                                                      
REMARK 465     GLY E    37                                                      
REMARK 465     GLU E    38                                                      
REMARK 465     LYS E    39                                                      
REMARK 465     ALA E    40                                                      
REMARK 465     PHE E    41                                                      
REMARK 465     TYR E    42                                                      
REMARK 465     ASN E   305                                                      
REMARK 465     SER E   306                                                      
REMARK 465     GLN E   307                                                      
REMARK 465     PRO E   308                                                      
REMARK 465     ALA E   309                                                      
REMARK 465     CYS E   310                                                      
REMARK 465     THR E   311                                                      
REMARK 465     ALA E   312                                                      
REMARK 465     ARG E   313                                                      
REMARK 465     ASP E   657                                                      
REMARK 465     LYS E   658                                                      
REMARK 465     PRO E   659                                                      
REMARK 465     SER E   660                                                      
REMARK 465     ASN F    35                                                      
REMARK 465     PRO F    36                                                      
REMARK 465     GLY F    37                                                      
REMARK 465     GLU F    38                                                      
REMARK 465     LYS F    39                                                      
REMARK 465     ALA F    40                                                      
REMARK 465     PHE F    41                                                      
REMARK 465     TYR F    42                                                      
REMARK 465     ASN F   305                                                      
REMARK 465     SER F   306                                                      
REMARK 465     GLN F   307                                                      
REMARK 465     PRO F   308                                                      
REMARK 465     ALA F   309                                                      
REMARK 465     CYS F   310                                                      
REMARK 465     THR F   311                                                      
REMARK 465     ALA F   312                                                      
REMARK 465     ARG F   313                                                      
REMARK 465     ASP F   657                                                      
REMARK 465     LYS F   658                                                      
REMARK 465     PRO F   659                                                      
REMARK 465     SER F   660                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A  47    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A  69    CG   CD   OE1  OE2                                  
REMARK 470     HIS A  86    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS A 137    CG   CD   CE   NZ                                   
REMARK 470     ARG A 200    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A 204    CG   OD1  OD2                                       
REMARK 470     HIS A 250    CG   ND1  CD2  CE1  NE2                             
REMARK 470     SER A 252    OG                                                  
REMARK 470     LYS A 253    CG   CD   CE   NZ                                   
REMARK 470     SER A 302    OG                                                  
REMARK 470     ARG A 303    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 404    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 442    CG   CD   CE   NZ                                   
REMARK 470     LYS A 611    CG   CD   CE   NZ                                   
REMARK 470     ASP A 615    OD1  OD2                                            
REMARK 470     GLU A 617    CG   CD   OE1  OE2                                  
REMARK 470     ARG B  47    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B  69    CG   CD   OE1  OE2                                  
REMARK 470     HIS B  86    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS B 137    CG   CD   CE   NZ                                   
REMARK 470     ARG B 200    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B 204    CG   OD1  OD2                                       
REMARK 470     HIS B 250    CG   ND1  CD2  CE1  NE2                             
REMARK 470     SER B 252    OG                                                  
REMARK 470     LYS B 253    CG   CD   CE   NZ                                   
REMARK 470     SER B 302    OG                                                  
REMARK 470     ARG B 303    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 404    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 442    CG   CD   CE   NZ                                   
REMARK 470     LYS B 611    CG   CD   CE   NZ                                   
REMARK 470     ASP B 615    OD1  OD2                                            
REMARK 470     GLU B 617    CG   CD   OE1  OE2                                  
REMARK 470     ARG C  47    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C  69    CG   CD   OE1  OE2                                  
REMARK 470     HIS C  86    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS C 137    CG   CD   CE   NZ                                   
REMARK 470     ARG C 200    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP C 204    CG   OD1  OD2                                       
REMARK 470     HIS C 250    CG   ND1  CD2  CE1  NE2                             
REMARK 470     SER C 252    OG                                                  
REMARK 470     LYS C 253    CG   CD   CE   NZ                                   
REMARK 470     SER C 302    OG                                                  
REMARK 470     ARG C 303    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C 404    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C 442    CG   CD   CE   NZ                                   
REMARK 470     LYS C 611    CG   CD   CE   NZ                                   
REMARK 470     ASP C 615    OD1  OD2                                            
REMARK 470     GLU C 617    CG   CD   OE1  OE2                                  
REMARK 470     ARG D  47    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU D  69    CG   CD   OE1  OE2                                  
REMARK 470     HIS D  86    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS D 137    CG   CD   CE   NZ                                   
REMARK 470     ARG D 200    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP D 204    CG   OD1  OD2                                       
REMARK 470     HIS D 250    CG   ND1  CD2  CE1  NE2                             
REMARK 470     SER D 252    OG                                                  
REMARK 470     LYS D 253    CG   CD   CE   NZ                                   
REMARK 470     SER D 302    OG                                                  
REMARK 470     ARG D 303    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN D 305    CG   OD1  ND2                                       
REMARK 470     GLN D 307    CG   CD   OE1  NE2                                  
REMARK 470     ARG D 313    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG D 404    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D 442    CG   CD   CE   NZ                                   
REMARK 470     LYS D 611    CG   CD   CE   NZ                                   
REMARK 470     ASP D 615    OD1  OD2                                            
REMARK 470     GLU D 617    CG   CD   OE1  OE2                                  
REMARK 470     ARG E  47    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU E  69    CG   CD   OE1  OE2                                  
REMARK 470     HIS E  86    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS E 137    CG   CD   CE   NZ                                   
REMARK 470     ARG E 200    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP E 204    CG   OD1  OD2                                       
REMARK 470     HIS E 250    CG   ND1  CD2  CE1  NE2                             
REMARK 470     SER E 252    OG                                                  
REMARK 470     LYS E 253    CG   CD   CE   NZ                                   
REMARK 470     SER E 302    OG                                                  
REMARK 470     ARG E 303    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG E 404    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS E 442    CG   CD   CE   NZ                                   
REMARK 470     LYS E 611    CG   CD   CE   NZ                                   
REMARK 470     ASP E 615    OD1  OD2                                            
REMARK 470     GLU E 617    CG   CD   OE1  OE2                                  
REMARK 470     ARG F  47    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU F  69    CG   CD   OE1  OE2                                  
REMARK 470     HIS F  86    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS F 137    CG   CD   CE   NZ                                   
REMARK 470     ARG F 200    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP F 204    CG   OD1  OD2                                       
REMARK 470     HIS F 250    CG   ND1  CD2  CE1  NE2                             
REMARK 470     SER F 252    OG                                                  
REMARK 470     LYS F 253    CG   CD   CE   NZ                                   
REMARK 470     SER F 302    OG                                                  
REMARK 470     ARG F 303    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG F 404    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS F 442    CG   CD   CE   NZ                                   
REMARK 470     LYS F 611    CG   CD   CE   NZ                                   
REMARK 470     ASP F 615    OD1  OD2                                            
REMARK 470     GLU F 617    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   ND2  ASN B   184     OE1  GLN C   171     1655     2.03            
REMARK 500   O    HIS B   182     NE2  HIS C   167     1655     2.13            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    HIS A   9     -162.67     56.01                                   
REMARK 500    SER A  75       72.40     50.46                                   
REMARK 500    ASP A  90      -63.53     -8.30                                   
REMARK 500    GLU A  91      -55.43    -29.15                                   
REMARK 500    ALA A 158      -57.27    -28.04                                   
REMARK 500    HIS A 182      -74.73   -111.34                                   
REMARK 500    GLU A 192      -33.87    -38.26                                   
REMARK 500    TRP A 210      -10.08    -46.77                                   
REMARK 500    ARG A 246      109.00   -173.54                                   
REMARK 500    HIS A 250       98.57    -51.23                                   
REMARK 500    ALA A 251      178.98    -55.03                                   
REMARK 500    SER A 252      109.77   -177.31                                   
REMARK 500    LYS A 253       -2.23    -55.36                                   
REMARK 500    ALA A 263       88.57   -166.78                                   
REMARK 500    THR A 295       -2.83    -57.27                                   
REMARK 500    GLN A 300       59.03    -57.64                                   
REMARK 500    SER A 302      135.70    -16.33                                   
REMARK 500    SER A 350       11.09   -152.67                                   
REMARK 500    ILE A 371      -54.39   -121.24                                   
REMARK 500    PHE A 410      -62.67   -101.14                                   
REMARK 500    SER A 431     -148.90    -81.54                                   
REMARK 500    MET A 438       43.05    -95.75                                   
REMARK 500    GLU A 481       19.47   -140.62                                   
REMARK 500    ASN A 492       65.64     34.21                                   
REMARK 500    ASP A 499     -162.73     71.95                                   
REMARK 500    ASN A 570       45.81    -93.02                                   
REMARK 500    LYS A 635      -51.23   -127.27                                   
REMARK 500    HIS B   9     -164.79     57.20                                   
REMARK 500    THR B  31     -158.62   -136.56                                   
REMARK 500    ALA B  58       51.39   -143.60                                   
REMARK 500    SER B  75       70.72     47.66                                   
REMARK 500    ASP B  90      -67.15     -8.03                                   
REMARK 500    GLU B  91      -57.20    -24.81                                   
REMARK 500    ALA B 115       38.33     73.12                                   
REMARK 500    THR B 128     -159.23   -152.13                                   
REMARK 500    ALA B 146      148.08   -172.23                                   
REMARK 500    HIS B 182      -70.24   -102.43                                   
REMARK 500    ILE B 188       97.00    -62.88                                   
REMARK 500    ALA B 189      162.59    -49.21                                   
REMARK 500    ARG B 191       79.01    -67.88                                   
REMARK 500    ARG B 246      102.02   -177.97                                   
REMARK 500    HIS B 250       93.60    -52.91                                   
REMARK 500    ALA B 251      178.90    -47.14                                   
REMARK 500    SER B 252      108.64   -179.02                                   
REMARK 500    LYS B 253       -3.61    -53.13                                   
REMARK 500    ALA B 263       88.25   -170.05                                   
REMARK 500    GLN B 300       56.24    -66.33                                   
REMARK 500    SER B 302      133.03    -17.12                                   
REMARK 500    SER B 350        7.23   -152.58                                   
REMARK 500    ILE B 371      -55.92   -120.97                                   
REMARK 500    PHE B 410      -62.76    -98.45                                   
REMARK 500    ARG B 424       70.15     41.34                                   
REMARK 500    SER B 431     -147.63    -79.74                                   
REMARK 500    MET B 438       44.32    -94.31                                   
REMARK 500    PRO B 459      -12.29    -48.79                                   
REMARK 500    GLU B 481       18.35   -140.00                                   
REMARK 500    ASN B 492       64.65     29.69                                   
REMARK 500    ASP B 499     -158.35     72.30                                   
REMARK 500    ASN B 570       45.45    -96.12                                   
REMARK 500    HIS C   9     -158.20     57.42                                   
REMARK 500    ALA C  58       54.48   -140.02                                   
REMARK 500    SER C  75       71.63     49.58                                   
REMARK 500    ASP C  90      -70.61     -6.82                                   
REMARK 500    GLU C  91      -58.42    -23.02                                   
REMARK 500    LEU C 108      152.90    -48.69                                   
REMARK 500    ALA C 115       39.65     72.27                                   
REMARK 500    ALA C 146      139.13   -177.82                                   
REMARK 500    LEU C 148      118.23   -160.26                                   
REMARK 500    ILE C 188       93.56    -67.19                                   
REMARK 500    ALA C 189      160.49    -45.80                                   
REMARK 500    GLU C 192      -30.78    -38.08                                   
REMARK 500    ARG C 246      111.87   -178.24                                   
REMARK 500    HIS C 250       98.29    -52.04                                   
REMARK 500    ALA C 251      178.39    -52.48                                   
REMARK 500    SER C 252      109.43   -177.09                                   
REMARK 500    LYS C 253       -7.19    -54.77                                   
REMARK 500    ALA C 263       91.55   -165.23                                   
REMARK 500    THR C 295       -5.48    -54.57                                   
REMARK 500    GLN C 300       52.64    -64.71                                   
REMARK 500    SER C 302      135.81    -23.80                                   
REMARK 500    SER C 350        9.99   -156.02                                   
REMARK 500    ILE C 371      -55.38   -126.94                                   
REMARK 500    PHE C 410      -64.92   -100.52                                   
REMARK 500    SER C 431     -151.39    -80.45                                   
REMARK 500    MET C 438       44.43    -97.82                                   
REMARK 500    LYS C 458       73.54   -118.14                                   
REMARK 500    PRO C 459       -9.72    -52.74                                   
REMARK 500    GLU C 481       18.12   -140.55                                   
REMARK 500    ASN C 492       67.10     29.37                                   
REMARK 500    ASP C 499     -161.03     73.55                                   
REMARK 500    ASN C 556       26.89     49.36                                   
REMARK 500    ASN C 570       45.16    -90.43                                   
REMARK 500    HIS D   9     -160.51     57.27                                   
REMARK 500    THR D  31     -157.38   -136.48                                   
REMARK 500    SER D  75       71.59     54.51                                   
REMARK 500    ASP D  90      -64.91     -4.47                                   
REMARK 500    GLU D  91      -54.74    -28.21                                   
REMARK 500    ALA D 115       36.55     73.60                                   
REMARK 500    THR D 128     -164.29   -162.59                                   
REMARK 500    HIS D 182      -60.30   -109.41                                   
REMARK 500    ILE D 188       88.72    -61.71                                   
REMARK 500    ALA D 189      166.53    -43.69                                   
REMARK 500    ARG D 191       76.25    -67.81                                   
REMARK 500    TRP D 210       -4.67    -55.12                                   
REMARK 500    ARG D 246      106.21   -179.04                                   
REMARK 500    HIS D 250       98.40    -51.31                                   
REMARK 500    ALA D 251      177.53    -55.93                                   
REMARK 500    SER D 252      114.85   -176.76                                   
REMARK 500    LYS D 253       -3.67    -57.91                                   
REMARK 500    ALA D 263       89.43   -170.16                                   
REMARK 500    SER D 302      129.10    -21.17                                   
REMARK 500    LEU D 304       -1.29     67.06                                   
REMARK 500    SER D 350       10.40   -153.24                                   
REMARK 500    ILE D 371      -56.71   -121.13                                   
REMARK 500    PHE D 410      -66.80   -102.98                                   
REMARK 500    SER D 431     -151.26    -81.25                                   
REMARK 500    MET D 438       44.01    -96.28                                   
REMARK 500    PRO D 459       -3.75    -56.46                                   
REMARK 500    GLU D 481       14.45   -143.94                                   
REMARK 500    ASN D 492       64.08     31.42                                   
REMARK 500    ASP D 499     -161.68     73.13                                   
REMARK 500    ASN D 570       45.50    -98.33                                   
REMARK 500    HIS E   9     -159.63     58.47                                   
REMARK 500    ALA E  58       54.64   -143.41                                   
REMARK 500    SER E  75       71.11     52.82                                   
REMARK 500    ASP E  90      -66.81     -3.72                                   
REMARK 500    GLU E  91      -54.77    -26.37                                   
REMARK 500    ALA E 115       39.34     70.30                                   
REMARK 500    THR E 128     -159.12   -157.03                                   
REMARK 500    ASP E 140       19.82     59.09                                   
REMARK 500    ALA E 146      147.98   -177.29                                   
REMARK 500    LEU E 148      115.69   -163.96                                   
REMARK 500    HIS E 182      -67.84   -107.36                                   
REMARK 500    ILE E 188       96.48    -62.67                                   
REMARK 500    ALA E 189      164.13    -48.66                                   
REMARK 500    ARG E 191       74.63    -64.42                                   
REMARK 500    GLU E 192      -31.52    -37.19                                   
REMARK 500    TRP E 210       -7.56    -51.61                                   
REMARK 500    ARG E 246      108.12   -177.43                                   
REMARK 500    HIS E 250      101.36    -57.19                                   
REMARK 500    ALA E 251      177.22    -54.56                                   
REMARK 500    SER E 252      106.40   -179.53                                   
REMARK 500    LYS E 253       -3.45    -52.61                                   
REMARK 500    ALA E 263       90.18   -166.28                                   
REMARK 500    GLN E 300       58.65    -63.81                                   
REMARK 500    SER E 302      128.75    -23.07                                   
REMARK 500    SER E 350        9.61   -154.78                                   
REMARK 500    ILE E 371      -56.15   -121.30                                   
REMARK 500    ALA E 391     -177.39   -175.77                                   
REMARK 500    PHE E 410      -67.48   -101.42                                   
REMARK 500    SER E 431     -151.07    -84.19                                   
REMARK 500    MET E 438       40.51    -90.11                                   
REMARK 500    LYS E 458       72.83   -119.20                                   
REMARK 500    GLU E 481       20.08   -143.65                                   
REMARK 500    ASN E 492       61.80     32.87                                   
REMARK 500    ASP E 499     -162.67     71.10                                   
REMARK 500    ASN E 570       45.74    -93.68                                   
REMARK 500    LYS E 635      -52.55   -129.16                                   
REMARK 500    HIS F   9     -164.78     52.97                                   
REMARK 500    SER F  75       73.22     49.40                                   
REMARK 500    ASP F  90      -63.30     -6.96                                   
REMARK 500    GLU F  91      -59.79    -27.17                                   
REMARK 500    LEU F 108      152.44    -46.18                                   
REMARK 500    THR F 128     -164.72   -161.76                                   
REMARK 500    ALA F 146      144.29   -175.73                                   
REMARK 500    HIS F 182      -67.99   -104.90                                   
REMARK 500    ILE F 188       90.27    -60.76                                   
REMARK 500    ALA F 189      166.80    -43.82                                   
REMARK 500    ARG F 191       75.73    -63.24                                   
REMARK 500    GLU F 192      -30.16    -38.08                                   
REMARK 500    TRP F 210       -7.31    -54.54                                   
REMARK 500    ARG F 246      109.80   -176.15                                   
REMARK 500    HIS F 250       98.89    -53.89                                   
REMARK 500    ALA F 251      176.75    -53.11                                   
REMARK 500    SER F 252      110.62   -174.60                                   
REMARK 500    LYS F 253       -3.02    -57.36                                   
REMARK 500    ALA F 263       88.48   -171.59                                   
REMARK 500    THR F 295       -3.95    -57.78                                   
REMARK 500    GLN F 300       57.76    -67.35                                   
REMARK 500    SER F 302      136.99    -19.76                                   
REMARK 500    SER F 350       11.20   -152.77                                   
REMARK 500    ILE F 371      -59.36   -123.32                                   
REMARK 500    PHE F 410      -65.05    -99.83                                   
REMARK 500    SER F 431     -151.37    -81.59                                   
REMARK 500    MET F 438       39.88    -96.94                                   
REMARK 500    LYS F 458       77.72   -117.16                                   
REMARK 500    GLU F 481       17.75   -144.02                                   
REMARK 500    ASN F 492       64.85     32.64                                   
REMARK 500    ASP F 499     -159.56     70.90                                   
REMARK 500    ASN F 570       44.60    -95.78                                   
REMARK 500    LYS F 635      -48.82   -130.12                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP A 1001                
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP B 1002                
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP C 1003                
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP D 1004                
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP E 1005                
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP F 1006                
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UGA A 1101                
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UGA B 1102                
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UGA C 1103                
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UGA D 1104                
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UGA E 1105                
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UGA F 1106                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1Z73   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1Z74   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1Z75   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1Z7B   RELATED DB: PDB                                   
DBREF  1Z7E A    1   660  UNP    P77398   ARNA_ECOLI       1    660             
DBREF  1Z7E B    1   660  UNP    P77398   ARNA_ECOLI       1    660             
DBREF  1Z7E C    1   660  UNP    P77398   ARNA_ECOLI       1    660             
DBREF  1Z7E D    1   660  UNP    P77398   ARNA_ECOLI       1    660             
DBREF  1Z7E E    1   660  UNP    P77398   ARNA_ECOLI       1    660             
DBREF  1Z7E F    1   660  UNP    P77398   ARNA_ECOLI       1    660             
SEQRES   1 A  660  MET LYS THR VAL VAL PHE ALA TYR HIS ASP MET GLY CYS          
SEQRES   2 A  660  LEU GLY ILE GLU ALA LEU LEU ALA ALA GLY TYR GLU ILE          
SEQRES   3 A  660  SER ALA ILE PHE THR HIS THR ASP ASN PRO GLY GLU LYS          
SEQRES   4 A  660  ALA PHE TYR GLY SER VAL ALA ARG LEU ALA ALA GLU ARG          
SEQRES   5 A  660  GLY ILE PRO VAL TYR ALA PRO ASP ASN VAL ASN HIS PRO          
SEQRES   6 A  660  LEU TRP VAL GLU ARG ILE ALA GLN LEU SER PRO ASP VAL          
SEQRES   7 A  660  ILE PHE SER PHE TYR TYR ARG HIS LEU ILE TYR ASP GLU          
SEQRES   8 A  660  ILE LEU GLN LEU ALA PRO ALA GLY ALA PHE ASN LEU HIS          
SEQRES   9 A  660  GLY SER LEU LEU PRO LYS TYR ARG GLY ARG ALA PRO LEU          
SEQRES  10 A  660  ASN TRP VAL LEU VAL ASN GLY GLU THR GLU THR GLY VAL          
SEQRES  11 A  660  THR LEU HIS ARG MET VAL LYS ARG ALA ASP ALA GLY ALA          
SEQRES  12 A  660  ILE VAL ALA GLN LEU ARG ILE ALA ILE ALA PRO ASP ASP          
SEQRES  13 A  660  ILE ALA ILE THR LEU HIS HIS LYS LEU CYS HIS ALA ALA          
SEQRES  14 A  660  ARG GLN LEU LEU GLU GLN THR LEU PRO ALA ILE LYS HIS          
SEQRES  15 A  660  GLY ASN ILE LEU GLU ILE ALA GLN ARG GLU ASN GLU ALA          
SEQRES  16 A  660  THR CYS PHE GLY ARG ARG THR PRO ASP ASP SER PHE LEU          
SEQRES  17 A  660  GLU TRP HIS LYS PRO ALA SER VAL LEU HIS ASN MET VAL          
SEQRES  18 A  660  ARG ALA VAL ALA ASP PRO TRP PRO GLY ALA PHE SER TYR          
SEQRES  19 A  660  VAL GLY ASN GLN LYS PHE THR VAL TRP SER SER ARG VAL          
SEQRES  20 A  660  HIS PRO HIS ALA SER LYS ALA GLN PRO GLY SER VAL ILE          
SEQRES  21 A  660  SER VAL ALA PRO LEU LEU ILE ALA CYS GLY ASP GLY ALA          
SEQRES  22 A  660  LEU GLU ILE VAL THR GLY GLN ALA GLY ASP GLY ILE THR          
SEQRES  23 A  660  MET GLN GLY SER GLN LEU ALA GLN THR LEU GLY LEU VAL          
SEQRES  24 A  660  GLN GLY SER ARG LEU ASN SER GLN PRO ALA CYS THR ALA          
SEQRES  25 A  660  ARG ARG ARG THR ARG VAL LEU ILE LEU GLY VAL ASN GLY          
SEQRES  26 A  660  PHE ILE GLY ASN HIS LEU THR GLU ARG LEU LEU ARG GLU          
SEQRES  27 A  660  ASP HIS TYR GLU VAL TYR GLY LEU ASP ILE GLY SER ASP          
SEQRES  28 A  660  ALA ILE SER ARG PHE LEU ASN HIS PRO HIS PHE HIS PHE          
SEQRES  29 A  660  VAL GLU GLY ASP ILE SER ILE HIS SER GLU TRP ILE GLU          
SEQRES  30 A  660  TYR HIS VAL LYS LYS CYS ASP VAL VAL LEU PRO LEU VAL          
SEQRES  31 A  660  ALA ILE ALA THR PRO ILE GLU TYR THR ARG ASN PRO LEU          
SEQRES  32 A  660  ARG VAL PHE GLU LEU ASP PHE GLU GLU ASN LEU ARG ILE          
SEQRES  33 A  660  ILE ARG TYR CYS VAL LYS TYR ARG LYS ARG ILE ILE PHE          
SEQRES  34 A  660  PRO SER THR SER GLU VAL TYR GLY MET CYS SER ASP LYS          
SEQRES  35 A  660  TYR PHE ASP GLU ASP HIS SER ASN LEU ILE VAL GLY PRO          
SEQRES  36 A  660  VAL ASN LYS PRO ARG TRP ILE TYR SER VAL SER LYS GLN          
SEQRES  37 A  660  LEU LEU ASP ARG VAL ILE TRP ALA TYR GLY GLU LYS GLU          
SEQRES  38 A  660  GLY LEU GLN PHE THR LEU PHE ARG PRO PHE ASN TRP MET          
SEQRES  39 A  660  GLY PRO ARG LEU ASP ASN LEU ASN ALA ALA ARG ILE GLY          
SEQRES  40 A  660  SER SER ARG ALA ILE THR GLN LEU ILE LEU ASN LEU VAL          
SEQRES  41 A  660  GLU GLY SER PRO ILE LYS LEU ILE ASP GLY GLY LYS GLN          
SEQRES  42 A  660  LYS ARG CYS PHE THR ASP ILE ARG ASP GLY ILE GLU ALA          
SEQRES  43 A  660  LEU TYR ARG ILE ILE GLU ASN ALA GLY ASN ARG CYS ASP          
SEQRES  44 A  660  GLY GLU ILE ILE ASN ILE GLY ASN PRO GLU ASN GLU ALA          
SEQRES  45 A  660  SER ILE GLU GLU LEU GLY GLU MET LEU LEU ALA SER PHE          
SEQRES  46 A  660  GLU LYS HIS PRO LEU ARG HIS HIS PHE PRO PRO PHE ALA          
SEQRES  47 A  660  GLY PHE ARG VAL VAL GLU SER SER SER TYR TYR GLY LYS          
SEQRES  48 A  660  GLY TYR GLN ASP VAL GLU HIS ARG LYS PRO SER ILE ARG          
SEQRES  49 A  660  ASN ALA HIS ARG CYS LEU ASP TRP GLU PRO LYS ILE ASP          
SEQRES  50 A  660  MET GLN GLU THR ILE ASP GLU THR LEU ASP PHE PHE LEU          
SEQRES  51 A  660  ARG THR VAL ASP LEU THR ASP LYS PRO SER                      
SEQRES   1 B  660  MET LYS THR VAL VAL PHE ALA TYR HIS ASP MET GLY CYS          
SEQRES   2 B  660  LEU GLY ILE GLU ALA LEU LEU ALA ALA GLY TYR GLU ILE          
SEQRES   3 B  660  SER ALA ILE PHE THR HIS THR ASP ASN PRO GLY GLU LYS          
SEQRES   4 B  660  ALA PHE TYR GLY SER VAL ALA ARG LEU ALA ALA GLU ARG          
SEQRES   5 B  660  GLY ILE PRO VAL TYR ALA PRO ASP ASN VAL ASN HIS PRO          
SEQRES   6 B  660  LEU TRP VAL GLU ARG ILE ALA GLN LEU SER PRO ASP VAL          
SEQRES   7 B  660  ILE PHE SER PHE TYR TYR ARG HIS LEU ILE TYR ASP GLU          
SEQRES   8 B  660  ILE LEU GLN LEU ALA PRO ALA GLY ALA PHE ASN LEU HIS          
SEQRES   9 B  660  GLY SER LEU LEU PRO LYS TYR ARG GLY ARG ALA PRO LEU          
SEQRES  10 B  660  ASN TRP VAL LEU VAL ASN GLY GLU THR GLU THR GLY VAL          
SEQRES  11 B  660  THR LEU HIS ARG MET VAL LYS ARG ALA ASP ALA GLY ALA          
SEQRES  12 B  660  ILE VAL ALA GLN LEU ARG ILE ALA ILE ALA PRO ASP ASP          
SEQRES  13 B  660  ILE ALA ILE THR LEU HIS HIS LYS LEU CYS HIS ALA ALA          
SEQRES  14 B  660  ARG GLN LEU LEU GLU GLN THR LEU PRO ALA ILE LYS HIS          
SEQRES  15 B  660  GLY ASN ILE LEU GLU ILE ALA GLN ARG GLU ASN GLU ALA          
SEQRES  16 B  660  THR CYS PHE GLY ARG ARG THR PRO ASP ASP SER PHE LEU          
SEQRES  17 B  660  GLU TRP HIS LYS PRO ALA SER VAL LEU HIS ASN MET VAL          
SEQRES  18 B  660  ARG ALA VAL ALA ASP PRO TRP PRO GLY ALA PHE SER TYR          
SEQRES  19 B  660  VAL GLY ASN GLN LYS PHE THR VAL TRP SER SER ARG VAL          
SEQRES  20 B  660  HIS PRO HIS ALA SER LYS ALA GLN PRO GLY SER VAL ILE          
SEQRES  21 B  660  SER VAL ALA PRO LEU LEU ILE ALA CYS GLY ASP GLY ALA          
SEQRES  22 B  660  LEU GLU ILE VAL THR GLY GLN ALA GLY ASP GLY ILE THR          
SEQRES  23 B  660  MET GLN GLY SER GLN LEU ALA GLN THR LEU GLY LEU VAL          
SEQRES  24 B  660  GLN GLY SER ARG LEU ASN SER GLN PRO ALA CYS THR ALA          
SEQRES  25 B  660  ARG ARG ARG THR ARG VAL LEU ILE LEU GLY VAL ASN GLY          
SEQRES  26 B  660  PHE ILE GLY ASN HIS LEU THR GLU ARG LEU LEU ARG GLU          
SEQRES  27 B  660  ASP HIS TYR GLU VAL TYR GLY LEU ASP ILE GLY SER ASP          
SEQRES  28 B  660  ALA ILE SER ARG PHE LEU ASN HIS PRO HIS PHE HIS PHE          
SEQRES  29 B  660  VAL GLU GLY ASP ILE SER ILE HIS SER GLU TRP ILE GLU          
SEQRES  30 B  660  TYR HIS VAL LYS LYS CYS ASP VAL VAL LEU PRO LEU VAL          
SEQRES  31 B  660  ALA ILE ALA THR PRO ILE GLU TYR THR ARG ASN PRO LEU          
SEQRES  32 B  660  ARG VAL PHE GLU LEU ASP PHE GLU GLU ASN LEU ARG ILE          
SEQRES  33 B  660  ILE ARG TYR CYS VAL LYS TYR ARG LYS ARG ILE ILE PHE          
SEQRES  34 B  660  PRO SER THR SER GLU VAL TYR GLY MET CYS SER ASP LYS          
SEQRES  35 B  660  TYR PHE ASP GLU ASP HIS SER ASN LEU ILE VAL GLY PRO          
SEQRES  36 B  660  VAL ASN LYS PRO ARG TRP ILE TYR SER VAL SER LYS GLN          
SEQRES  37 B  660  LEU LEU ASP ARG VAL ILE TRP ALA TYR GLY GLU LYS GLU          
SEQRES  38 B  660  GLY LEU GLN PHE THR LEU PHE ARG PRO PHE ASN TRP MET          
SEQRES  39 B  660  GLY PRO ARG LEU ASP ASN LEU ASN ALA ALA ARG ILE GLY          
SEQRES  40 B  660  SER SER ARG ALA ILE THR GLN LEU ILE LEU ASN LEU VAL          
SEQRES  41 B  660  GLU GLY SER PRO ILE LYS LEU ILE ASP GLY GLY LYS GLN          
SEQRES  42 B  660  LYS ARG CYS PHE THR ASP ILE ARG ASP GLY ILE GLU ALA          
SEQRES  43 B  660  LEU TYR ARG ILE ILE GLU ASN ALA GLY ASN ARG CYS ASP          
SEQRES  44 B  660  GLY GLU ILE ILE ASN ILE GLY ASN PRO GLU ASN GLU ALA          
SEQRES  45 B  660  SER ILE GLU GLU LEU GLY GLU MET LEU LEU ALA SER PHE          
SEQRES  46 B  660  GLU LYS HIS PRO LEU ARG HIS HIS PHE PRO PRO PHE ALA          
SEQRES  47 B  660  GLY PHE ARG VAL VAL GLU SER SER SER TYR TYR GLY LYS          
SEQRES  48 B  660  GLY TYR GLN ASP VAL GLU HIS ARG LYS PRO SER ILE ARG          
SEQRES  49 B  660  ASN ALA HIS ARG CYS LEU ASP TRP GLU PRO LYS ILE ASP          
SEQRES  50 B  660  MET GLN GLU THR ILE ASP GLU THR LEU ASP PHE PHE LEU          
SEQRES  51 B  660  ARG THR VAL ASP LEU THR ASP LYS PRO SER                      
SEQRES   1 C  660  MET LYS THR VAL VAL PHE ALA TYR HIS ASP MET GLY CYS          
SEQRES   2 C  660  LEU GLY ILE GLU ALA LEU LEU ALA ALA GLY TYR GLU ILE          
SEQRES   3 C  660  SER ALA ILE PHE THR HIS THR ASP ASN PRO GLY GLU LYS          
SEQRES   4 C  660  ALA PHE TYR GLY SER VAL ALA ARG LEU ALA ALA GLU ARG          
SEQRES   5 C  660  GLY ILE PRO VAL TYR ALA PRO ASP ASN VAL ASN HIS PRO          
SEQRES   6 C  660  LEU TRP VAL GLU ARG ILE ALA GLN LEU SER PRO ASP VAL          
SEQRES   7 C  660  ILE PHE SER PHE TYR TYR ARG HIS LEU ILE TYR ASP GLU          
SEQRES   8 C  660  ILE LEU GLN LEU ALA PRO ALA GLY ALA PHE ASN LEU HIS          
SEQRES   9 C  660  GLY SER LEU LEU PRO LYS TYR ARG GLY ARG ALA PRO LEU          
SEQRES  10 C  660  ASN TRP VAL LEU VAL ASN GLY GLU THR GLU THR GLY VAL          
SEQRES  11 C  660  THR LEU HIS ARG MET VAL LYS ARG ALA ASP ALA GLY ALA          
SEQRES  12 C  660  ILE VAL ALA GLN LEU ARG ILE ALA ILE ALA PRO ASP ASP          
SEQRES  13 C  660  ILE ALA ILE THR LEU HIS HIS LYS LEU CYS HIS ALA ALA          
SEQRES  14 C  660  ARG GLN LEU LEU GLU GLN THR LEU PRO ALA ILE LYS HIS          
SEQRES  15 C  660  GLY ASN ILE LEU GLU ILE ALA GLN ARG GLU ASN GLU ALA          
SEQRES  16 C  660  THR CYS PHE GLY ARG ARG THR PRO ASP ASP SER PHE LEU          
SEQRES  17 C  660  GLU TRP HIS LYS PRO ALA SER VAL LEU HIS ASN MET VAL          
SEQRES  18 C  660  ARG ALA VAL ALA ASP PRO TRP PRO GLY ALA PHE SER TYR          
SEQRES  19 C  660  VAL GLY ASN GLN LYS PHE THR VAL TRP SER SER ARG VAL          
SEQRES  20 C  660  HIS PRO HIS ALA SER LYS ALA GLN PRO GLY SER VAL ILE          
SEQRES  21 C  660  SER VAL ALA PRO LEU LEU ILE ALA CYS GLY ASP GLY ALA          
SEQRES  22 C  660  LEU GLU ILE VAL THR GLY GLN ALA GLY ASP GLY ILE THR          
SEQRES  23 C  660  MET GLN GLY SER GLN LEU ALA GLN THR LEU GLY LEU VAL          
SEQRES  24 C  660  GLN GLY SER ARG LEU ASN SER GLN PRO ALA CYS THR ALA          
SEQRES  25 C  660  ARG ARG ARG THR ARG VAL LEU ILE LEU GLY VAL ASN GLY          
SEQRES  26 C  660  PHE ILE GLY ASN HIS LEU THR GLU ARG LEU LEU ARG GLU          
SEQRES  27 C  660  ASP HIS TYR GLU VAL TYR GLY LEU ASP ILE GLY SER ASP          
SEQRES  28 C  660  ALA ILE SER ARG PHE LEU ASN HIS PRO HIS PHE HIS PHE          
SEQRES  29 C  660  VAL GLU GLY ASP ILE SER ILE HIS SER GLU TRP ILE GLU          
SEQRES  30 C  660  TYR HIS VAL LYS LYS CYS ASP VAL VAL LEU PRO LEU VAL          
SEQRES  31 C  660  ALA ILE ALA THR PRO ILE GLU TYR THR ARG ASN PRO LEU          
SEQRES  32 C  660  ARG VAL PHE GLU LEU ASP PHE GLU GLU ASN LEU ARG ILE          
SEQRES  33 C  660  ILE ARG TYR CYS VAL LYS TYR ARG LYS ARG ILE ILE PHE          
SEQRES  34 C  660  PRO SER THR SER GLU VAL TYR GLY MET CYS SER ASP LYS          
SEQRES  35 C  660  TYR PHE ASP GLU ASP HIS SER ASN LEU ILE VAL GLY PRO          
SEQRES  36 C  660  VAL ASN LYS PRO ARG TRP ILE TYR SER VAL SER LYS GLN          
SEQRES  37 C  660  LEU LEU ASP ARG VAL ILE TRP ALA TYR GLY GLU LYS GLU          
SEQRES  38 C  660  GLY LEU GLN PHE THR LEU PHE ARG PRO PHE ASN TRP MET          
SEQRES  39 C  660  GLY PRO ARG LEU ASP ASN LEU ASN ALA ALA ARG ILE GLY          
SEQRES  40 C  660  SER SER ARG ALA ILE THR GLN LEU ILE LEU ASN LEU VAL          
SEQRES  41 C  660  GLU GLY SER PRO ILE LYS LEU ILE ASP GLY GLY LYS GLN          
SEQRES  42 C  660  LYS ARG CYS PHE THR ASP ILE ARG ASP GLY ILE GLU ALA          
SEQRES  43 C  660  LEU TYR ARG ILE ILE GLU ASN ALA GLY ASN ARG CYS ASP          
SEQRES  44 C  660  GLY GLU ILE ILE ASN ILE GLY ASN PRO GLU ASN GLU ALA          
SEQRES  45 C  660  SER ILE GLU GLU LEU GLY GLU MET LEU LEU ALA SER PHE          
SEQRES  46 C  660  GLU LYS HIS PRO LEU ARG HIS HIS PHE PRO PRO PHE ALA          
SEQRES  47 C  660  GLY PHE ARG VAL VAL GLU SER SER SER TYR TYR GLY LYS          
SEQRES  48 C  660  GLY TYR GLN ASP VAL GLU HIS ARG LYS PRO SER ILE ARG          
SEQRES  49 C  660  ASN ALA HIS ARG CYS LEU ASP TRP GLU PRO LYS ILE ASP          
SEQRES  50 C  660  MET GLN GLU THR ILE ASP GLU THR LEU ASP PHE PHE LEU          
SEQRES  51 C  660  ARG THR VAL ASP LEU THR ASP LYS PRO SER                      
SEQRES   1 D  660  MET LYS THR VAL VAL PHE ALA TYR HIS ASP MET GLY CYS          
SEQRES   2 D  660  LEU GLY ILE GLU ALA LEU LEU ALA ALA GLY TYR GLU ILE          
SEQRES   3 D  660  SER ALA ILE PHE THR HIS THR ASP ASN PRO GLY GLU LYS          
SEQRES   4 D  660  ALA PHE TYR GLY SER VAL ALA ARG LEU ALA ALA GLU ARG          
SEQRES   5 D  660  GLY ILE PRO VAL TYR ALA PRO ASP ASN VAL ASN HIS PRO          
SEQRES   6 D  660  LEU TRP VAL GLU ARG ILE ALA GLN LEU SER PRO ASP VAL          
SEQRES   7 D  660  ILE PHE SER PHE TYR TYR ARG HIS LEU ILE TYR ASP GLU          
SEQRES   8 D  660  ILE LEU GLN LEU ALA PRO ALA GLY ALA PHE ASN LEU HIS          
SEQRES   9 D  660  GLY SER LEU LEU PRO LYS TYR ARG GLY ARG ALA PRO LEU          
SEQRES  10 D  660  ASN TRP VAL LEU VAL ASN GLY GLU THR GLU THR GLY VAL          
SEQRES  11 D  660  THR LEU HIS ARG MET VAL LYS ARG ALA ASP ALA GLY ALA          
SEQRES  12 D  660  ILE VAL ALA GLN LEU ARG ILE ALA ILE ALA PRO ASP ASP          
SEQRES  13 D  660  ILE ALA ILE THR LEU HIS HIS LYS LEU CYS HIS ALA ALA          
SEQRES  14 D  660  ARG GLN LEU LEU GLU GLN THR LEU PRO ALA ILE LYS HIS          
SEQRES  15 D  660  GLY ASN ILE LEU GLU ILE ALA GLN ARG GLU ASN GLU ALA          
SEQRES  16 D  660  THR CYS PHE GLY ARG ARG THR PRO ASP ASP SER PHE LEU          
SEQRES  17 D  660  GLU TRP HIS LYS PRO ALA SER VAL LEU HIS ASN MET VAL          
SEQRES  18 D  660  ARG ALA VAL ALA ASP PRO TRP PRO GLY ALA PHE SER TYR          
SEQRES  19 D  660  VAL GLY ASN GLN LYS PHE THR VAL TRP SER SER ARG VAL          
SEQRES  20 D  660  HIS PRO HIS ALA SER LYS ALA GLN PRO GLY SER VAL ILE          
SEQRES  21 D  660  SER VAL ALA PRO LEU LEU ILE ALA CYS GLY ASP GLY ALA          
SEQRES  22 D  660  LEU GLU ILE VAL THR GLY GLN ALA GLY ASP GLY ILE THR          
SEQRES  23 D  660  MET GLN GLY SER GLN LEU ALA GLN THR LEU GLY LEU VAL          
SEQRES  24 D  660  GLN GLY SER ARG LEU ASN SER GLN PRO ALA CYS THR ALA          
SEQRES  25 D  660  ARG ARG ARG THR ARG VAL LEU ILE LEU GLY VAL ASN GLY          
SEQRES  26 D  660  PHE ILE GLY ASN HIS LEU THR GLU ARG LEU LEU ARG GLU          
SEQRES  27 D  660  ASP HIS TYR GLU VAL TYR GLY LEU ASP ILE GLY SER ASP          
SEQRES  28 D  660  ALA ILE SER ARG PHE LEU ASN HIS PRO HIS PHE HIS PHE          
SEQRES  29 D  660  VAL GLU GLY ASP ILE SER ILE HIS SER GLU TRP ILE GLU          
SEQRES  30 D  660  TYR HIS VAL LYS LYS CYS ASP VAL VAL LEU PRO LEU VAL          
SEQRES  31 D  660  ALA ILE ALA THR PRO ILE GLU TYR THR ARG ASN PRO LEU          
SEQRES  32 D  660  ARG VAL PHE GLU LEU ASP PHE GLU GLU ASN LEU ARG ILE          
SEQRES  33 D  660  ILE ARG TYR CYS VAL LYS TYR ARG LYS ARG ILE ILE PHE          
SEQRES  34 D  660  PRO SER THR SER GLU VAL TYR GLY MET CYS SER ASP LYS          
SEQRES  35 D  660  TYR PHE ASP GLU ASP HIS SER ASN LEU ILE VAL GLY PRO          
SEQRES  36 D  660  VAL ASN LYS PRO ARG TRP ILE TYR SER VAL SER LYS GLN          
SEQRES  37 D  660  LEU LEU ASP ARG VAL ILE TRP ALA TYR GLY GLU LYS GLU          
SEQRES  38 D  660  GLY LEU GLN PHE THR LEU PHE ARG PRO PHE ASN TRP MET          
SEQRES  39 D  660  GLY PRO ARG LEU ASP ASN LEU ASN ALA ALA ARG ILE GLY          
SEQRES  40 D  660  SER SER ARG ALA ILE THR GLN LEU ILE LEU ASN LEU VAL          
SEQRES  41 D  660  GLU GLY SER PRO ILE LYS LEU ILE ASP GLY GLY LYS GLN          
SEQRES  42 D  660  LYS ARG CYS PHE THR ASP ILE ARG ASP GLY ILE GLU ALA          
SEQRES  43 D  660  LEU TYR ARG ILE ILE GLU ASN ALA GLY ASN ARG CYS ASP          
SEQRES  44 D  660  GLY GLU ILE ILE ASN ILE GLY ASN PRO GLU ASN GLU ALA          
SEQRES  45 D  660  SER ILE GLU GLU LEU GLY GLU MET LEU LEU ALA SER PHE          
SEQRES  46 D  660  GLU LYS HIS PRO LEU ARG HIS HIS PHE PRO PRO PHE ALA          
SEQRES  47 D  660  GLY PHE ARG VAL VAL GLU SER SER SER TYR TYR GLY LYS          
SEQRES  48 D  660  GLY TYR GLN ASP VAL GLU HIS ARG LYS PRO SER ILE ARG          
SEQRES  49 D  660  ASN ALA HIS ARG CYS LEU ASP TRP GLU PRO LYS ILE ASP          
SEQRES  50 D  660  MET GLN GLU THR ILE ASP GLU THR LEU ASP PHE PHE LEU          
SEQRES  51 D  660  ARG THR VAL ASP LEU THR ASP LYS PRO SER                      
SEQRES   1 E  660  MET LYS THR VAL VAL PHE ALA TYR HIS ASP MET GLY CYS          
SEQRES   2 E  660  LEU GLY ILE GLU ALA LEU LEU ALA ALA GLY TYR GLU ILE          
SEQRES   3 E  660  SER ALA ILE PHE THR HIS THR ASP ASN PRO GLY GLU LYS          
SEQRES   4 E  660  ALA PHE TYR GLY SER VAL ALA ARG LEU ALA ALA GLU ARG          
SEQRES   5 E  660  GLY ILE PRO VAL TYR ALA PRO ASP ASN VAL ASN HIS PRO          
SEQRES   6 E  660  LEU TRP VAL GLU ARG ILE ALA GLN LEU SER PRO ASP VAL          
SEQRES   7 E  660  ILE PHE SER PHE TYR TYR ARG HIS LEU ILE TYR ASP GLU          
SEQRES   8 E  660  ILE LEU GLN LEU ALA PRO ALA GLY ALA PHE ASN LEU HIS          
SEQRES   9 E  660  GLY SER LEU LEU PRO LYS TYR ARG GLY ARG ALA PRO LEU          
SEQRES  10 E  660  ASN TRP VAL LEU VAL ASN GLY GLU THR GLU THR GLY VAL          
SEQRES  11 E  660  THR LEU HIS ARG MET VAL LYS ARG ALA ASP ALA GLY ALA          
SEQRES  12 E  660  ILE VAL ALA GLN LEU ARG ILE ALA ILE ALA PRO ASP ASP          
SEQRES  13 E  660  ILE ALA ILE THR LEU HIS HIS LYS LEU CYS HIS ALA ALA          
SEQRES  14 E  660  ARG GLN LEU LEU GLU GLN THR LEU PRO ALA ILE LYS HIS          
SEQRES  15 E  660  GLY ASN ILE LEU GLU ILE ALA GLN ARG GLU ASN GLU ALA          
SEQRES  16 E  660  THR CYS PHE GLY ARG ARG THR PRO ASP ASP SER PHE LEU          
SEQRES  17 E  660  GLU TRP HIS LYS PRO ALA SER VAL LEU HIS ASN MET VAL          
SEQRES  18 E  660  ARG ALA VAL ALA ASP PRO TRP PRO GLY ALA PHE SER TYR          
SEQRES  19 E  660  VAL GLY ASN GLN LYS PHE THR VAL TRP SER SER ARG VAL          
SEQRES  20 E  660  HIS PRO HIS ALA SER LYS ALA GLN PRO GLY SER VAL ILE          
SEQRES  21 E  660  SER VAL ALA PRO LEU LEU ILE ALA CYS GLY ASP GLY ALA          
SEQRES  22 E  660  LEU GLU ILE VAL THR GLY GLN ALA GLY ASP GLY ILE THR          
SEQRES  23 E  660  MET GLN GLY SER GLN LEU ALA GLN THR LEU GLY LEU VAL          
SEQRES  24 E  660  GLN GLY SER ARG LEU ASN SER GLN PRO ALA CYS THR ALA          
SEQRES  25 E  660  ARG ARG ARG THR ARG VAL LEU ILE LEU GLY VAL ASN GLY          
SEQRES  26 E  660  PHE ILE GLY ASN HIS LEU THR GLU ARG LEU LEU ARG GLU          
SEQRES  27 E  660  ASP HIS TYR GLU VAL TYR GLY LEU ASP ILE GLY SER ASP          
SEQRES  28 E  660  ALA ILE SER ARG PHE LEU ASN HIS PRO HIS PHE HIS PHE          
SEQRES  29 E  660  VAL GLU GLY ASP ILE SER ILE HIS SER GLU TRP ILE GLU          
SEQRES  30 E  660  TYR HIS VAL LYS LYS CYS ASP VAL VAL LEU PRO LEU VAL          
SEQRES  31 E  660  ALA ILE ALA THR PRO ILE GLU TYR THR ARG ASN PRO LEU          
SEQRES  32 E  660  ARG VAL PHE GLU LEU ASP PHE GLU GLU ASN LEU ARG ILE          
SEQRES  33 E  660  ILE ARG TYR CYS VAL LYS TYR ARG LYS ARG ILE ILE PHE          
SEQRES  34 E  660  PRO SER THR SER GLU VAL TYR GLY MET CYS SER ASP LYS          
SEQRES  35 E  660  TYR PHE ASP GLU ASP HIS SER ASN LEU ILE VAL GLY PRO          
SEQRES  36 E  660  VAL ASN LYS PRO ARG TRP ILE TYR SER VAL SER LYS GLN          
SEQRES  37 E  660  LEU LEU ASP ARG VAL ILE TRP ALA TYR GLY GLU LYS GLU          
SEQRES  38 E  660  GLY LEU GLN PHE THR LEU PHE ARG PRO PHE ASN TRP MET          
SEQRES  39 E  660  GLY PRO ARG LEU ASP ASN LEU ASN ALA ALA ARG ILE GLY          
SEQRES  40 E  660  SER SER ARG ALA ILE THR GLN LEU ILE LEU ASN LEU VAL          
SEQRES  41 E  660  GLU GLY SER PRO ILE LYS LEU ILE ASP GLY GLY LYS GLN          
SEQRES  42 E  660  LYS ARG CYS PHE THR ASP ILE ARG ASP GLY ILE GLU ALA          
SEQRES  43 E  660  LEU TYR ARG ILE ILE GLU ASN ALA GLY ASN ARG CYS ASP          
SEQRES  44 E  660  GLY GLU ILE ILE ASN ILE GLY ASN PRO GLU ASN GLU ALA          
SEQRES  45 E  660  SER ILE GLU GLU LEU GLY GLU MET LEU LEU ALA SER PHE          
SEQRES  46 E  660  GLU LYS HIS PRO LEU ARG HIS HIS PHE PRO PRO PHE ALA          
SEQRES  47 E  660  GLY PHE ARG VAL VAL GLU SER SER SER TYR TYR GLY LYS          
SEQRES  48 E  660  GLY TYR GLN ASP VAL GLU HIS ARG LYS PRO SER ILE ARG          
SEQRES  49 E  660  ASN ALA HIS ARG CYS LEU ASP TRP GLU PRO LYS ILE ASP          
SEQRES  50 E  660  MET GLN GLU THR ILE ASP GLU THR LEU ASP PHE PHE LEU          
SEQRES  51 E  660  ARG THR VAL ASP LEU THR ASP LYS PRO SER                      
SEQRES   1 F  660  MET LYS THR VAL VAL PHE ALA TYR HIS ASP MET GLY CYS          
SEQRES   2 F  660  LEU GLY ILE GLU ALA LEU LEU ALA ALA GLY TYR GLU ILE          
SEQRES   3 F  660  SER ALA ILE PHE THR HIS THR ASP ASN PRO GLY GLU LYS          
SEQRES   4 F  660  ALA PHE TYR GLY SER VAL ALA ARG LEU ALA ALA GLU ARG          
SEQRES   5 F  660  GLY ILE PRO VAL TYR ALA PRO ASP ASN VAL ASN HIS PRO          
SEQRES   6 F  660  LEU TRP VAL GLU ARG ILE ALA GLN LEU SER PRO ASP VAL          
SEQRES   7 F  660  ILE PHE SER PHE TYR TYR ARG HIS LEU ILE TYR ASP GLU          
SEQRES   8 F  660  ILE LEU GLN LEU ALA PRO ALA GLY ALA PHE ASN LEU HIS          
SEQRES   9 F  660  GLY SER LEU LEU PRO LYS TYR ARG GLY ARG ALA PRO LEU          
SEQRES  10 F  660  ASN TRP VAL LEU VAL ASN GLY GLU THR GLU THR GLY VAL          
SEQRES  11 F  660  THR LEU HIS ARG MET VAL LYS ARG ALA ASP ALA GLY ALA          
SEQRES  12 F  660  ILE VAL ALA GLN LEU ARG ILE ALA ILE ALA PRO ASP ASP          
SEQRES  13 F  660  ILE ALA ILE THR LEU HIS HIS LYS LEU CYS HIS ALA ALA          
SEQRES  14 F  660  ARG GLN LEU LEU GLU GLN THR LEU PRO ALA ILE LYS HIS          
SEQRES  15 F  660  GLY ASN ILE LEU GLU ILE ALA GLN ARG GLU ASN GLU ALA          
SEQRES  16 F  660  THR CYS PHE GLY ARG ARG THR PRO ASP ASP SER PHE LEU          
SEQRES  17 F  660  GLU TRP HIS LYS PRO ALA SER VAL LEU HIS ASN MET VAL          
SEQRES  18 F  660  ARG ALA VAL ALA ASP PRO TRP PRO GLY ALA PHE SER TYR          
SEQRES  19 F  660  VAL GLY ASN GLN LYS PHE THR VAL TRP SER SER ARG VAL          
SEQRES  20 F  660  HIS PRO HIS ALA SER LYS ALA GLN PRO GLY SER VAL ILE          
SEQRES  21 F  660  SER VAL ALA PRO LEU LEU ILE ALA CYS GLY ASP GLY ALA          
SEQRES  22 F  660  LEU GLU ILE VAL THR GLY GLN ALA GLY ASP GLY ILE THR          
SEQRES  23 F  660  MET GLN GLY SER GLN LEU ALA GLN THR LEU GLY LEU VAL          
SEQRES  24 F  660  GLN GLY SER ARG LEU ASN SER GLN PRO ALA CYS THR ALA          
SEQRES  25 F  660  ARG ARG ARG THR ARG VAL LEU ILE LEU GLY VAL ASN GLY          
SEQRES  26 F  660  PHE ILE GLY ASN HIS LEU THR GLU ARG LEU LEU ARG GLU          
SEQRES  27 F  660  ASP HIS TYR GLU VAL TYR GLY LEU ASP ILE GLY SER ASP          
SEQRES  28 F  660  ALA ILE SER ARG PHE LEU ASN HIS PRO HIS PHE HIS PHE          
SEQRES  29 F  660  VAL GLU GLY ASP ILE SER ILE HIS SER GLU TRP ILE GLU          
SEQRES  30 F  660  TYR HIS VAL LYS LYS CYS ASP VAL VAL LEU PRO LEU VAL          
SEQRES  31 F  660  ALA ILE ALA THR PRO ILE GLU TYR THR ARG ASN PRO LEU          
SEQRES  32 F  660  ARG VAL PHE GLU LEU ASP PHE GLU GLU ASN LEU ARG ILE          
SEQRES  33 F  660  ILE ARG TYR CYS VAL LYS TYR ARG LYS ARG ILE ILE PHE          
SEQRES  34 F  660  PRO SER THR SER GLU VAL TYR GLY MET CYS SER ASP LYS          
SEQRES  35 F  660  TYR PHE ASP GLU ASP HIS SER ASN LEU ILE VAL GLY PRO          
SEQRES  36 F  660  VAL ASN LYS PRO ARG TRP ILE TYR SER VAL SER LYS GLN          
SEQRES  37 F  660  LEU LEU ASP ARG VAL ILE TRP ALA TYR GLY GLU LYS GLU          
SEQRES  38 F  660  GLY LEU GLN PHE THR LEU PHE ARG PRO PHE ASN TRP MET          
SEQRES  39 F  660  GLY PRO ARG LEU ASP ASN LEU ASN ALA ALA ARG ILE GLY          
SEQRES  40 F  660  SER SER ARG ALA ILE THR GLN LEU ILE LEU ASN LEU VAL          
SEQRES  41 F  660  GLU GLY SER PRO ILE LYS LEU ILE ASP GLY GLY LYS GLN          
SEQRES  42 F  660  LYS ARG CYS PHE THR ASP ILE ARG ASP GLY ILE GLU ALA          
SEQRES  43 F  660  LEU TYR ARG ILE ILE GLU ASN ALA GLY ASN ARG CYS ASP          
SEQRES  44 F  660  GLY GLU ILE ILE ASN ILE GLY ASN PRO GLU ASN GLU ALA          
SEQRES  45 F  660  SER ILE GLU GLU LEU GLY GLU MET LEU LEU ALA SER PHE          
SEQRES  46 F  660  GLU LYS HIS PRO LEU ARG HIS HIS PHE PRO PRO PHE ALA          
SEQRES  47 F  660  GLY PHE ARG VAL VAL GLU SER SER SER TYR TYR GLY LYS          
SEQRES  48 F  660  GLY TYR GLN ASP VAL GLU HIS ARG LYS PRO SER ILE ARG          
SEQRES  49 F  660  ASN ALA HIS ARG CYS LEU ASP TRP GLU PRO LYS ILE ASP          
SEQRES  50 F  660  MET GLN GLU THR ILE ASP GLU THR LEU ASP PHE PHE LEU          
SEQRES  51 F  660  ARG THR VAL ASP LEU THR ASP LYS PRO SER                      
HET    ATP  A1001      31                                                       
HET    ATP  B1002      31                                                       
HET    ATP  C1003      31                                                       
HET    ATP  D1004      31                                                       
HET    ATP  E1005      31                                                       
HET    ATP  F1006      31                                                       
HET    UGA  A1101      37                                                       
HET    UGA  B1102      37                                                       
HET    UGA  C1103      37                                                       
HET    UGA  D1104      37                                                       
HET    UGA  E1105      37                                                       
HET    UGA  F1106      37                                                       
HETNAM     ATP ADENOSINE-5'-TRIPHOSPHATE                                        
HETNAM     UGA URIDINE-5'-DIPHOSPHATE-GLUCURONIC ACID                           
HETSYN     UGA UDP-GLUCURONIC ACID                                              
FORMUL   7  ATP    6(C10 H16 N5 O13 P3)                                         
FORMUL  13  UGA    6(C15 H22 N2 O18 P2)                                         
HELIX    1   1 TYR A    8  ALA A   22  1                                  15    
HELIX    2   2 SER A   44  GLY A   53  1                                  10    
HELIX    3   3 HIS A   64  SER A   75  1                                  12    
HELIX    4   4 TYR A   89  GLN A   94  1                                   6    
HELIX    5   5 ALA A  115  ASN A  123  1                                   9    
HELIX    6   6 ILE A  157  LYS A  181  1                                  25    
HELIX    7   7 ARG A  191  ALA A  195  5                                   5    
HELIX    8   8 THR A  202  PHE A  207  5                                   6    
HELIX    9   9 PRO A  213  VAL A  224  1                                  12    
HELIX   10  10 GLY A  289  THR A  295  1                                   7    
HELIX   11  11 GLY A  325  GLU A  338  1                                  14    
HELIX   12  12 ILE A  353  LEU A  357  5                                   5    
HELIX   13  13 HIS A  372  CYS A  383  1                                  12    
HELIX   14  14 PRO A  395  ASN A  401  1                                   7    
HELIX   15  15 ASN A  401  PHE A  410  1                                  10    
HELIX   16  16 PHE A  410  TYR A  423  1                                  14    
HELIX   17  17 THR A  432  GLY A  437  5                                   6    
HELIX   18  18 ARG A  460  GLY A  482  1                                  23    
HELIX   19  19 ASN A  500  ARG A  505  1                                   6    
HELIX   20  20 ARG A  510  GLY A  522  1                                  13    
HELIX   21  21 GLY A  530  LYS A  532  5                                   3    
HELIX   22  22 ILE A  540  ASN A  553  1                                  14    
HELIX   23  23 ALA A  554  ARG A  557  5                                   4    
HELIX   24  24 ASN A  567  GLU A  569  5                                   3    
HELIX   25  25 ILE A  574  HIS A  588  1                                  15    
HELIX   26  26 LEU A  590  PHE A  594  5                                   5    
HELIX   27  27 SER A  605  GLY A  610  1                                   6    
HELIX   28  28 ILE A  623  ASP A  631  1                                   9    
HELIX   29  29 ASP A  637  ARG A  651  1                                  15    
HELIX   30  30 TYR B    8  ALA B   22  1                                  15    
HELIX   31  31 SER B   44  ARG B   52  1                                   9    
HELIX   32  32 HIS B   64  SER B   75  1                                  12    
HELIX   33  33 TYR B   89  GLN B   94  1                                   6    
HELIX   34  34 ALA B  115  ASN B  123  1                                   9    
HELIX   35  35 ILE B  157  GLY B  183  1                                  27    
HELIX   36  36 ARG B  191  ALA B  195  5                                   5    
HELIX   37  37 THR B  202  PHE B  207  5                                   6    
HELIX   38  38 PRO B  213  VAL B  224  1                                  12    
HELIX   39  39 GLY B  289  LEU B  296  1                                   8    
HELIX   40  40 GLY B  325  GLU B  338  1                                  14    
HELIX   41  41 ILE B  353  LEU B  357  5                                   5    
HELIX   42  42 HIS B  372  CYS B  383  1                                  12    
HELIX   43  43 PRO B  395  ASN B  401  1                                   7    
HELIX   44  44 ASN B  401  PHE B  410  1                                  10    
HELIX   45  45 PHE B  410  TYR B  423  1                                  14    
HELIX   46  46 THR B  432  GLY B  437  5                                   6    
HELIX   47  47 ARG B  460  GLY B  482  1                                  23    
HELIX   48  48 ASN B  500  ARG B  505  1                                   6    
HELIX   49  49 ARG B  510  GLY B  522  1                                  13    
HELIX   50  50 GLY B  530  LYS B  532  5                                   3    
HELIX   51  51 ILE B  540  ASN B  553  1                                  14    
HELIX   52  52 ALA B  554  ARG B  557  5                                   4    
HELIX   53  53 ASN B  567  GLU B  569  5                                   3    
HELIX   54  54 ILE B  574  HIS B  588  1                                  15    
HELIX   55  55 PRO B  589  PHE B  594  5                                   6    
HELIX   56  56 SER B  605  GLY B  610  1                                   6    
HELIX   57  57 ILE B  623  ASP B  631  1                                   9    
HELIX   58  58 ASP B  637  ARG B  651  1                                  15    
HELIX   59  59 TYR C    8  ALA C   22  1                                  15    
HELIX   60  60 SER C   44  ARG C   52  1                                   9    
HELIX   61  61 HIS C   64  SER C   75  1                                  12    
HELIX   62  62 TYR C   89  GLN C   94  1                                   6    
HELIX   63  63 ALA C  115  ASN C  123  1                                   9    
HELIX   64  64 ILE C  157  GLY C  183  1                                  27    
HELIX   65  65 THR C  202  PHE C  207  5                                   6    
HELIX   66  66 PRO C  213  VAL C  224  1                                  12    
HELIX   67  67 GLY C  289  THR C  295  1                                   7    
HELIX   68  68 GLY C  325  GLU C  338  1                                  14    
HELIX   69  69 ILE C  353  LEU C  357  5                                   5    
HELIX   70  70 HIS C  372  CYS C  383  1                                  12    
HELIX   71  71 PRO C  395  ASN C  401  1                                   7    
HELIX   72  72 ASN C  401  PHE C  410  1                                  10    
HELIX   73  73 PHE C  410  TYR C  423  1                                  14    
HELIX   74  74 THR C  432  GLY C  437  5                                   6    
HELIX   75  75 ARG C  460  GLY C  482  1                                  23    
HELIX   76  76 ASN C  500  ARG C  505  1                                   6    
HELIX   77  77 ARG C  510  GLY C  522  1                                  13    
HELIX   78  78 GLY C  530  LYS C  532  5                                   3    
HELIX   79  79 ILE C  540  ASN C  553  1                                  14    
HELIX   80  80 ALA C  554  ARG C  557  5                                   4    
HELIX   81  81 ASN C  567  GLU C  569  5                                   3    
HELIX   82  82 ILE C  574  HIS C  588  1                                  15    
HELIX   83  83 LEU C  590  PHE C  594  5                                   5    
HELIX   84  84 SER C  605  GLY C  610  1                                   6    
HELIX   85  85 ILE C  623  ASP C  631  1                                   9    
HELIX   86  86 ASP C  637  ARG C  651  1                                  15    
HELIX   87  87 TYR D    8  ALA D   22  1                                  15    
HELIX   88  88 SER D   44  GLY D   53  1                                  10    
HELIX   89  89 HIS D   64  SER D   75  1                                  12    
HELIX   90  90 TYR D   89  GLN D   94  1                                   6    
HELIX   91  91 ALA D  115  ASN D  123  1                                   9    
HELIX   92  92 ILE D  157  GLY D  183  1                                  27    
HELIX   93  93 THR D  202  PHE D  207  5                                   6    
HELIX   94  94 PRO D  213  VAL D  224  1                                  12    
HELIX   95  95 GLY D  289  GLY D  297  1                                   9    
HELIX   96  96 GLY D  325  GLU D  338  1                                  14    
HELIX   97  97 ILE D  353  LEU D  357  5                                   5    
HELIX   98  98 HIS D  372  CYS D  383  1                                  12    
HELIX   99  99 PRO D  395  ASN D  401  1                                   7    
HELIX  100 100 ASN D  401  PHE D  410  1                                  10    
HELIX  101 101 PHE D  410  TYR D  423  1                                  14    
HELIX  102 102 THR D  432  GLY D  437  5                                   6    
HELIX  103 103 ARG D  460  GLY D  482  1                                  23    
HELIX  104 104 ASN D  500  ARG D  505  1                                   6    
HELIX  105 105 ARG D  510  GLY D  522  1                                  13    
HELIX  106 106 GLY D  530  LYS D  532  5                                   3    
HELIX  107 107 ILE D  540  ASN D  553  1                                  14    
HELIX  108 108 ALA D  554  ARG D  557  5                                   4    
HELIX  109 109 ASN D  567  GLU D  569  5                                   3    
HELIX  110 110 ILE D  574  HIS D  588  1                                  15    
HELIX  111 111 LEU D  590  PHE D  594  5                                   5    
HELIX  112 112 SER D  605  GLY D  610  1                                   6    
HELIX  113 113 ILE D  623  ASP D  631  1                                   9    
HELIX  114 114 ASP D  637  ARG D  651  1                                  15    
HELIX  115 115 TYR E    8  ALA E   22  1                                  15    
HELIX  116 116 SER E   44  ARG E   52  1                                   9    
HELIX  117 117 HIS E   64  SER E   75  1                                  12    
HELIX  118 118 TYR E   89  GLN E   94  1                                   6    
HELIX  119 119 ALA E  115  ASN E  123  1                                   9    
HELIX  120 120 ILE E  157  GLY E  183  1                                  27    
HELIX  121 121 THR E  202  PHE E  207  5                                   6    
HELIX  122 122 PRO E  213  VAL E  224  1                                  12    
HELIX  123 123 GLY E  289  GLY E  297  1                                   9    
HELIX  124 124 GLY E  325  GLU E  338  1                                  14    
HELIX  125 125 ILE E  353  LEU E  357  5                                   5    
HELIX  126 126 HIS E  372  CYS E  383  1                                  12    
HELIX  127 127 PRO E  395  ASN E  401  1                                   7    
HELIX  128 128 ASN E  401  PHE E  410  1                                  10    
HELIX  129 129 PHE E  410  TYR E  423  1                                  14    
HELIX  130 130 THR E  432  GLY E  437  5                                   6    
HELIX  131 131 ARG E  460  GLY E  482  1                                  23    
HELIX  132 132 ASN E  500  ARG E  505  1                                   6    
HELIX  133 133 ARG E  510  GLY E  522  1                                  13    
HELIX  134 134 GLY E  530  LYS E  532  5                                   3    
HELIX  135 135 ILE E  540  ASN E  553  1                                  14    
HELIX  136 136 ALA E  554  ARG E  557  5                                   4    
HELIX  137 137 ASN E  567  GLU E  569  5                                   3    
HELIX  138 138 ILE E  574  HIS E  588  1                                  15    
HELIX  139 139 PRO E  589  PHE E  594  5                                   6    
HELIX  140 140 SER E  605  GLY E  610  1                                   6    
HELIX  141 141 ILE E  623  ASP E  631  1                                   9    
HELIX  142 142 ASP E  637  ARG E  651  1                                  15    
HELIX  143 143 TYR F    8  ALA F   22  1                                  15    
HELIX  144 144 SER F   44  ARG F   52  1                                   9    
HELIX  145 145 HIS F   64  SER F   75  1                                  12    
HELIX  146 146 TYR F   89  GLN F   94  1                                   6    
HELIX  147 147 ALA F  115  ASN F  123  1                                   9    
HELIX  148 148 ILE F  157  GLY F  183  1                                  27    
HELIX  149 149 THR F  202  PHE F  207  5                                   6    
HELIX  150 150 PRO F  213  VAL F  224  1                                  12    
HELIX  151 151 GLY F  289  LEU F  296  1                                   8    
HELIX  152 152 GLY F  325  GLU F  338  1                                  14    
HELIX  153 153 ILE F  353  LEU F  357  5                                   5    
HELIX  154 154 HIS F  372  CYS F  383  1                                  12    
HELIX  155 155 THR F  394  ASN F  401  1                                   8    
HELIX  156 156 ASN F  401  PHE F  410  1                                  10    
HELIX  157 157 PHE F  410  TYR F  423  1                                  14    
HELIX  158 158 THR F  432  GLY F  437  5                                   6    
HELIX  159 159 ARG F  460  GLY F  482  1                                  23    
HELIX  160 160 ASN F  500  ARG F  505  1                                   6    
HELIX  161 161 ARG F  510  GLY F  522  1                                  13    
HELIX  162 162 GLY F  530  LYS F  532  5                                   3    
HELIX  163 163 ILE F  540  ASN F  553  1                                  14    
HELIX  164 164 ALA F  554  ARG F  557  5                                   4    
HELIX  165 165 ASN F  567  GLU F  569  5                                   3    
HELIX  166 166 ILE F  574  HIS F  588  1                                  15    
HELIX  167 167 LEU F  590  PHE F  594  5                                   5    
HELIX  168 168 SER F  605  GLY F  610  1                                   6    
HELIX  169 169 ILE F  623  ASP F  631  1                                   9    
HELIX  170 170 ASP F  637  ARG F  651  1                                  15    
SHEET    1   A 7 VAL A  56  TYR A  57  0                                        
SHEET    2   A 7 GLU A  25  PHE A  30  1  N  ILE A  29   O  TYR A  57           
SHEET    3   A 7 LYS A   2  ALA A   7  1  N  VAL A   5   O  PHE A  30           
SHEET    4   A 7 VAL A  78  PHE A  82  1  O  PHE A  80   N  PHE A   6           
SHEET    5   A 7 ALA A 100  HIS A 104  1  O  PHE A 101   N  ILE A  79           
SHEET    6   A 7 GLU A 127  ARG A 134 -1  O  HIS A 133   N  ASN A 102           
SHEET    7   A 7 ILE A 144  ALA A 151 -1  O  ILE A 150   N  THR A 128           
SHEET    1   B 4 ALA A 231  VAL A 235  0                                        
SHEET    2   B 4 GLN A 238  SER A 244 -1  O  GLN A 238   N  VAL A 235           
SHEET    3   B 4 THR A 278  ALA A 281 -1  O  GLN A 280   N  THR A 241           
SHEET    4   B 4 MET A 287  GLN A 288 -1  O  MET A 287   N  GLY A 279           
SHEET    1   C 4 VAL A 247  HIS A 248  0                                        
SHEET    2   C 4 ALA A 273  ILE A 276 -1  O  ALA A 273   N  HIS A 248           
SHEET    3   C 4 LEU A 265  ALA A 268 -1  N  LEU A 265   O  ILE A 276           
SHEET    4   C 4 VAL A 259  SER A 261 -1  N  ILE A 260   O  LEU A 266           
SHEET    1   D 7 PHE A 362  GLU A 366  0                                        
SHEET    2   D 7 TYR A 341  ASP A 347  1  N  VAL A 343   O  HIS A 363           
SHEET    3   D 7 THR A 316  LEU A 321  1  N  ILE A 320   O  TYR A 344           
SHEET    4   D 7 VAL A 385  PRO A 388  1  O  LEU A 387   N  LEU A 319           
SHEET    5   D 7 ARG A 426  PRO A 430  1  O  ILE A 428   N  VAL A 386           
SHEET    6   D 7 PHE A 485  PRO A 490  1  O  PHE A 488   N  PHE A 429           
SHEET    7   D 7 GLU A 561  ILE A 565  1  O  ILE A 563   N  LEU A 487           
SHEET    1   E 2 LEU A 451  VAL A 453  0                                        
SHEET    2   E 2 LEU D 451  VAL D 453 -1  O  VAL D 453   N  LEU A 451           
SHEET    1   F 2 TRP A 493  MET A 494  0                                        
SHEET    2   F 2 THR A 538  ASP A 539  1  O  THR A 538   N  MET A 494           
SHEET    1   G 2 ILE A 525  ILE A 528  0                                        
SHEET    2   G 2 PHE A 600  VAL A 603  1  O  ARG A 601   N  ILE A 525           
SHEET    1   H 2 LYS A 534  CYS A 536  0                                        
SHEET    2   H 2 GLU A 571  SER A 573 -1  O  ALA A 572   N  ARG A 535           
SHEET    1   I 7 VAL B  56  TYR B  57  0                                        
SHEET    2   I 7 GLU B  25  PHE B  30  1  N  ILE B  29   O  TYR B  57           
SHEET    3   I 7 LYS B   2  ALA B   7  1  N  VAL B   5   O  PHE B  30           
SHEET    4   I 7 VAL B  78  PHE B  82  1  O  PHE B  80   N  PHE B   6           
SHEET    5   I 7 ALA B 100  HIS B 104  1  O  PHE B 101   N  ILE B  79           
SHEET    6   I 7 GLU B 127  ARG B 134 -1  O  HIS B 133   N  ASN B 102           
SHEET    7   I 7 ILE B 144  ALA B 151 -1  O  ALA B 146   N  LEU B 132           
SHEET    1   J 4 ALA B 231  VAL B 235  0                                        
SHEET    2   J 4 GLN B 238  SER B 244 -1  O  VAL B 242   N  ALA B 231           
SHEET    3   J 4 THR B 278  ALA B 281 -1  O  THR B 278   N  TRP B 243           
SHEET    4   J 4 MET B 287  GLN B 288 -1  O  MET B 287   N  GLY B 279           
SHEET    1   K 4 VAL B 247  HIS B 248  0                                        
SHEET    2   K 4 ALA B 273  ILE B 276 -1  O  ALA B 273   N  HIS B 248           
SHEET    3   K 4 LEU B 265  ALA B 268 -1  N  ILE B 267   O  LEU B 274           
SHEET    4   K 4 VAL B 259  SER B 261 -1  N  ILE B 260   O  LEU B 266           
SHEET    1   L 7 PHE B 362  GLU B 366  0                                        
SHEET    2   L 7 TYR B 341  ASP B 347  1  N  VAL B 343   O  HIS B 363           
SHEET    3   L 7 THR B 316  LEU B 321  1  N  ILE B 320   O  TYR B 344           
SHEET    4   L 7 VAL B 385  PRO B 388  1  O  VAL B 385   N  LEU B 319           
SHEET    5   L 7 ARG B 426  PRO B 430  1  O  ILE B 428   N  VAL B 386           
SHEET    6   L 7 PHE B 485  PRO B 490  1  O  PHE B 488   N  PHE B 429           
SHEET    7   L 7 GLU B 561  ILE B 565  1  O  ILE B 563   N  LEU B 487           
SHEET    1   M 2 LEU B 451  VAL B 453  0                                        
SHEET    2   M 2 LEU E 451  VAL E 453 -1  O  VAL E 453   N  LEU B 451           
SHEET    1   N 2 TRP B 493  MET B 494  0                                        
SHEET    2   N 2 THR B 538  ASP B 539  1  O  THR B 538   N  MET B 494           
SHEET    1   O 2 ILE B 525  ILE B 528  0                                        
SHEET    2   O 2 PHE B 600  VAL B 603  1  O  ARG B 601   N  ILE B 525           
SHEET    1   P 2 LYS B 534  CYS B 536  0                                        
SHEET    2   P 2 GLU B 571  SER B 573 -1  O  ALA B 572   N  ARG B 535           
SHEET    1   Q 7 VAL C  56  TYR C  57  0                                        
SHEET    2   Q 7 GLU C  25  PHE C  30  1  N  ILE C  29   O  TYR C  57           
SHEET    3   Q 7 LYS C   2  ALA C   7  1  N  VAL C   5   O  PHE C  30           
SHEET    4   Q 7 VAL C  78  PHE C  82  1  O  PHE C  80   N  PHE C   6           
SHEET    5   Q 7 ALA C 100  HIS C 104  1  O  PHE C 101   N  ILE C  79           
SHEET    6   Q 7 GLU C 127  ARG C 134 -1  O  HIS C 133   N  ASN C 102           
SHEET    7   Q 7 ILE C 144  ALA C 151 -1  O  ALA C 146   N  LEU C 132           
SHEET    1   R 4 ALA C 231  VAL C 235  0                                        
SHEET    2   R 4 GLN C 238  SER C 244 -1  O  GLN C 238   N  VAL C 235           
SHEET    3   R 4 THR C 278  ALA C 281 -1  O  THR C 278   N  TRP C 243           
SHEET    4   R 4 MET C 287  GLN C 288 -1  O  MET C 287   N  GLY C 279           
SHEET    1   S 4 VAL C 247  HIS C 248  0                                        
SHEET    2   S 4 ALA C 273  ILE C 276 -1  O  ALA C 273   N  HIS C 248           
SHEET    3   S 4 LEU C 265  ALA C 268 -1  N  LEU C 265   O  ILE C 276           
SHEET    4   S 4 VAL C 259  SER C 261 -1  N  ILE C 260   O  LEU C 266           
SHEET    1   T 7 PHE C 362  GLU C 366  0                                        
SHEET    2   T 7 TYR C 341  ASP C 347  1  N  VAL C 343   O  HIS C 363           
SHEET    3   T 7 THR C 316  LEU C 321  1  N  ILE C 320   O  TYR C 344           
SHEET    4   T 7 VAL C 385  PRO C 388  1  O  VAL C 385   N  LEU C 319           
SHEET    5   T 7 ARG C 426  PRO C 430  1  O  ARG C 426   N  VAL C 386           
SHEET    6   T 7 PHE C 485  PRO C 490  1  O  PHE C 488   N  PHE C 429           
SHEET    7   T 7 GLU C 561  ILE C 565  1  O  ILE C 563   N  LEU C 487           
SHEET    1   U 2 LEU C 451  VAL C 453  0                                        
SHEET    2   U 2 LEU F 451  VAL F 453 -1  O  VAL F 453   N  LEU C 451           
SHEET    1   V 2 TRP C 493  MET C 494  0                                        
SHEET    2   V 2 THR C 538  ASP C 539  1  O  THR C 538   N  MET C 494           
SHEET    1   W 2 ILE C 525  ILE C 528  0                                        
SHEET    2   W 2 PHE C 600  VAL C 603  1  O  ARG C 601   N  ILE C 525           
SHEET    1   X 2 LYS C 534  CYS C 536  0                                        
SHEET    2   X 2 GLU C 571  SER C 573 -1  O  ALA C 572   N  ARG C 535           
SHEET    1   Y 7 VAL D  56  TYR D  57  0                                        
SHEET    2   Y 7 GLU D  25  PHE D  30  1  N  ILE D  29   O  TYR D  57           
SHEET    3   Y 7 LYS D   2  ALA D   7  1  N  VAL D   5   O  PHE D  30           
SHEET    4   Y 7 VAL D  78  PHE D  82  1  O  PHE D  82   N  PHE D   6           
SHEET    5   Y 7 ALA D 100  HIS D 104  1  O  LEU D 103   N  SER D  81           
SHEET    6   Y 7 GLU D 127  ARG D 134 -1  O  THR D 131   N  HIS D 104           
SHEET    7   Y 7 ILE D 144  ALA D 151 -1  O  ILE D 150   N  THR D 128           
SHEET    1   Z 4 ALA D 231  VAL D 235  0                                        
SHEET    2   Z 4 GLN D 238  SER D 244 -1  O  GLN D 238   N  VAL D 235           
SHEET    3   Z 4 THR D 278  ALA D 281 -1  O  GLN D 280   N  THR D 241           
SHEET    4   Z 4 MET D 287  GLN D 288 -1  O  MET D 287   N  GLY D 279           
SHEET    1  AA 4 VAL D 247  HIS D 248  0                                        
SHEET    2  AA 4 ALA D 273  ILE D 276 -1  O  ALA D 273   N  HIS D 248           
SHEET    3  AA 4 LEU D 265  ALA D 268 -1  N  ILE D 267   O  LEU D 274           
SHEET    4  AA 4 VAL D 259  SER D 261 -1  N  ILE D 260   O  LEU D 266           
SHEET    1  AB 7 PHE D 362  GLU D 366  0                                        
SHEET    2  AB 7 TYR D 341  ASP D 347  1  N  VAL D 343   O  HIS D 363           
SHEET    3  AB 7 THR D 316  LEU D 321  1  N  ILE D 320   O  TYR D 344           
SHEET    4  AB 7 VAL D 385  PRO D 388  1  O  VAL D 385   N  LEU D 319           
SHEET    5  AB 7 ARG D 426  PRO D 430  1  O  ILE D 428   N  VAL D 386           
SHEET    6  AB 7 PHE D 485  PRO D 490  1  O  PHE D 488   N  PHE D 429           
SHEET    7  AB 7 GLU D 561  ILE D 565  1  O  ILE D 563   N  LEU D 487           
SHEET    1  AC 2 TRP D 493  MET D 494  0                                        
SHEET    2  AC 2 THR D 538  ASP D 539  1  O  THR D 538   N  MET D 494           
SHEET    1  AD 2 ILE D 525  ILE D 528  0                                        
SHEET    2  AD 2 PHE D 600  VAL D 603  1  O  ARG D 601   N  LEU D 527           
SHEET    1  AE 2 LYS D 534  CYS D 536  0                                        
SHEET    2  AE 2 GLU D 571  SER D 573 -1  O  ALA D 572   N  ARG D 535           
SHEET    1  AF 7 VAL E  56  TYR E  57  0                                        
SHEET    2  AF 7 GLU E  25  PHE E  30  1  N  ILE E  29   O  TYR E  57           
SHEET    3  AF 7 LYS E   2  ALA E   7  1  N  VAL E   5   O  PHE E  30           
SHEET    4  AF 7 VAL E  78  PHE E  82  1  O  PHE E  80   N  PHE E   6           
SHEET    5  AF 7 GLY E  99  HIS E 104  1  O  PHE E 101   N  ILE E  79           
SHEET    6  AF 7 GLU E 127  ARG E 134 -1  O  HIS E 133   N  ASN E 102           
SHEET    7  AF 7 ILE E 144  ALA E 151 -1  O  ILE E 150   N  THR E 128           
SHEET    1  AG 4 ALA E 231  VAL E 235  0                                        
SHEET    2  AG 4 GLN E 238  SER E 244 -1  O  GLN E 238   N  VAL E 235           
SHEET    3  AG 4 THR E 278  ALA E 281 -1  O  THR E 278   N  TRP E 243           
SHEET    4  AG 4 MET E 287  GLN E 288 -1  O  MET E 287   N  GLY E 279           
SHEET    1  AH 4 VAL E 247  HIS E 248  0                                        
SHEET    2  AH 4 ALA E 273  ILE E 276 -1  O  ALA E 273   N  HIS E 248           
SHEET    3  AH 4 LEU E 265  ALA E 268 -1  N  ILE E 267   O  LEU E 274           
SHEET    4  AH 4 VAL E 259  SER E 261 -1  N  ILE E 260   O  LEU E 266           
SHEET    1  AI 7 PHE E 362  GLU E 366  0                                        
SHEET    2  AI 7 TYR E 341  ASP E 347  1  N  VAL E 343   O  HIS E 363           
SHEET    3  AI 7 THR E 316  LEU E 321  1  N  ILE E 320   O  TYR E 344           
SHEET    4  AI 7 VAL E 385  PRO E 388  1  O  VAL E 385   N  LEU E 319           
SHEET    5  AI 7 ARG E 426  PRO E 430  1  O  ILE E 428   N  VAL E 386           
SHEET    6  AI 7 PHE E 485  PRO E 490  1  O  PHE E 488   N  PHE E 429           
SHEET    7  AI 7 GLU E 561  ILE E 565  1  O  ILE E 563   N  LEU E 487           
SHEET    1  AJ 2 TRP E 493  MET E 494  0                                        
SHEET    2  AJ 2 THR E 538  ASP E 539  1  O  THR E 538   N  MET E 494           
SHEET    1  AK 2 ILE E 525  ILE E 528  0                                        
SHEET    2  AK 2 PHE E 600  VAL E 603  1  O  ARG E 601   N  ILE E 525           
SHEET    1  AL 2 LYS E 534  CYS E 536  0                                        
SHEET    2  AL 2 GLU E 571  SER E 573 -1  O  ALA E 572   N  ARG E 535           
SHEET    1  AM 7 VAL F  56  TYR F  57  0                                        
SHEET    2  AM 7 GLU F  25  PHE F  30  1  N  ILE F  29   O  TYR F  57           
SHEET    3  AM 7 LYS F   2  ALA F   7  1  N  THR F   3   O  GLU F  25           
SHEET    4  AM 7 VAL F  78  PHE F  82  1  O  PHE F  80   N  PHE F   6           
SHEET    5  AM 7 ALA F 100  HIS F 104  1  O  LEU F 103   N  SER F  81           
SHEET    6  AM 7 GLU F 127  ARG F 134 -1  O  THR F 131   N  HIS F 104           
SHEET    7  AM 7 ILE F 144  ALA F 151 -1  O  ILE F 150   N  THR F 128           
SHEET    1  AN 4 ALA F 231  VAL F 235  0                                        
SHEET    2  AN 4 GLN F 238  SER F 244 -1  O  GLN F 238   N  VAL F 235           
SHEET    3  AN 4 THR F 278  ALA F 281 -1  O  THR F 278   N  TRP F 243           
SHEET    4  AN 4 MET F 287  GLN F 288 -1  O  MET F 287   N  GLY F 279           
SHEET    1  AO 4 VAL F 247  HIS F 248  0                                        
SHEET    2  AO 4 ALA F 273  ILE F 276 -1  O  ALA F 273   N  HIS F 248           
SHEET    3  AO 4 LEU F 265  ALA F 268 -1  N  LEU F 265   O  ILE F 276           
SHEET    4  AO 4 VAL F 259  SER F 261 -1  N  ILE F 260   O  LEU F 266           
SHEET    1  AP 7 PHE F 362  GLU F 366  0                                        
SHEET    2  AP 7 TYR F 341  ASP F 347  1  N  VAL F 343   O  HIS F 363           
SHEET    3  AP 7 THR F 316  LEU F 321  1  N  ILE F 320   O  TYR F 344           
SHEET    4  AP 7 VAL F 385  PRO F 388  1  O  VAL F 385   N  LEU F 319           
SHEET    5  AP 7 ARG F 426  PRO F 430  1  O  ILE F 428   N  VAL F 386           
SHEET    6  AP 7 PHE F 485  PRO F 490  1  O  PHE F 488   N  PHE F 429           
SHEET    7  AP 7 GLU F 561  ILE F 565  1  O  ILE F 563   N  LEU F 487           
SHEET    1  AQ 2 TRP F 493  MET F 494  0                                        
SHEET    2  AQ 2 THR F 538  ASP F 539  1  O  THR F 538   N  MET F 494           
SHEET    1  AR 2 ILE F 525  ILE F 528  0                                        
SHEET    2  AR 2 PHE F 600  VAL F 603  1  O  ARG F 601   N  LEU F 527           
SHEET    1  AS 2 LYS F 534  CYS F 536  0                                        
SHEET    2  AS 2 GLU F 571  SER F 573 -1  O  ALA F 572   N  ARG F 535           
CISPEP   1 LEU A  108    PRO A  109          0         0.38                     
CISPEP   2 ASP A  226    PRO A  227          0         0.21                     
CISPEP   3 ALA A  263    PRO A  264          0         0.25                     
CISPEP   4 LEU B  108    PRO B  109          0         0.38                     
CISPEP   5 ASP B  226    PRO B  227          0         0.04                     
CISPEP   6 ALA B  263    PRO B  264          0         0.07                     
CISPEP   7 LEU C  108    PRO C  109          0         0.19                     
CISPEP   8 ASP C  226    PRO C  227          0         0.12                     
CISPEP   9 ALA C  263    PRO C  264          0         0.07                     
CISPEP  10 LEU D  108    PRO D  109          0         0.29                     
CISPEP  11 ASP D  226    PRO D  227          0         0.02                     
CISPEP  12 ALA D  263    PRO D  264          0         0.12                     
CISPEP  13 LEU E  108    PRO E  109          0         0.17                     
CISPEP  14 ASP E  226    PRO E  227          0         0.38                     
CISPEP  15 ALA E  263    PRO E  264          0         0.11                     
CISPEP  16 LEU F  108    PRO F  109          0         0.22                     
CISPEP  17 ASP F  226    PRO F  227          0         0.12                     
CISPEP  18 ALA F  263    PRO F  264          0         0.23                     
SITE     1 AC1 13 ASN A 324  GLY A 325  PHE A 326  ILE A 327                    
SITE     2 AC1 13 ASP A 347  ILE A 348  GLY A 367  ASP A 368                    
SITE     3 AC1 13 ILE A 369  LEU A 389  VAL A 390  ALA A 393                    
SITE     4 AC1 13 ARG A 510                                                     
SITE     1 AC2 13 ASN B 324  GLY B 325  PHE B 326  ILE B 327                    
SITE     2 AC2 13 ASP B 347  ILE B 348  GLY B 367  ASP B 368                    
SITE     3 AC2 13 ILE B 369  LEU B 389  VAL B 390  ALA B 393                    
SITE     4 AC2 13 ARG B 510                                                     
SITE     1 AC3 12 GLY C 322  GLY C 325  PHE C 326  ILE C 327                    
SITE     2 AC3 12 ASP C 347  ILE C 348  GLY C 367  ASP C 368                    
SITE     3 AC3 12 ILE C 369  LEU C 389  VAL C 390  ARG C 510                    
SITE     1 AC4 11 GLY D 325  PHE D 326  ILE D 327  ASP D 347                    
SITE     2 AC4 11 ILE D 348  GLY D 367  ASP D 368  ILE D 369                    
SITE     3 AC4 11 LEU D 389  VAL D 390  ARG D 510                               
SITE     1 AC5 11 GLY E 325  PHE E 326  ILE E 327  ASP E 347                    
SITE     2 AC5 11 ILE E 348  GLY E 367  ASP E 368  ILE E 369                    
SITE     3 AC5 11 LEU E 389  VAL E 390  ARG E 510                               
SITE     1 AC6 13 ASN F 324  GLY F 325  PHE F 326  ILE F 327                    
SITE     2 AC6 13 ASP F 347  ILE F 348  GLY F 367  ASP F 368                    
SITE     3 AC6 13 ILE F 369  LEU F 389  VAL F 390  ALA F 393                    
SITE     4 AC6 13 ARG F 510                                                     
SITE     1 AC7 24 ALA A 393  PRO A 395  TYR A 398  THR A 432                    
SITE     2 AC7 24 SER A 433  GLU A 434  ARG A 460  TYR A 463                    
SITE     3 AC7 24 PRO A 490  PHE A 491  ASN A 492  ARG A 510                    
SITE     4 AC7 24 ALA A 511  GLN A 514  LYS A 526  LEU A 527                    
SITE     5 AC7 24 ILE A 528  GLN A 533  ARG A 535  ILE A 574                    
SITE     6 AC7 24 TYR A 609  TYR A 613  ASP A 615  ARG A 619                    
SITE     1 AC8 24 ALA B 393  PRO B 395  TYR B 398  THR B 432                    
SITE     2 AC8 24 SER B 433  GLU B 434  ARG B 460  TYR B 463                    
SITE     3 AC8 24 PRO B 490  PHE B 491  ASN B 492  ARG B 510                    
SITE     4 AC8 24 ALA B 511  GLN B 514  LYS B 526  LEU B 527                    
SITE     5 AC8 24 ILE B 528  GLN B 533  ARG B 535  ILE B 574                    
SITE     6 AC8 24 TYR B 609  TYR B 613  ASP B 615  ARG B 619                    
SITE     1 AC9 24 ALA C 393  PRO C 395  TYR C 398  THR C 432                    
SITE     2 AC9 24 SER C 433  GLU C 434  ARG C 460  TYR C 463                    
SITE     3 AC9 24 PRO C 490  PHE C 491  ASN C 492  ARG C 510                    
SITE     4 AC9 24 ALA C 511  GLN C 514  LYS C 526  LEU C 527                    
SITE     5 AC9 24 ILE C 528  GLN C 533  ARG C 535  ILE C 574                    
SITE     6 AC9 24 TYR C 609  TYR C 613  ASP C 615  ARG C 619                    
SITE     1 BC1 24 ALA D 393  PRO D 395  TYR D 398  THR D 432                    
SITE     2 BC1 24 SER D 433  GLU D 434  ARG D 460  TYR D 463                    
SITE     3 BC1 24 PRO D 490  PHE D 491  ASN D 492  ARG D 510                    
SITE     4 BC1 24 ALA D 511  GLN D 514  LYS D 526  LEU D 527                    
SITE     5 BC1 24 ILE D 528  GLN D 533  ARG D 535  ILE D 574                    
SITE     6 BC1 24 TYR D 609  TYR D 613  ASP D 615  ARG D 619                    
SITE     1 BC2 24 ALA E 393  PRO E 395  TYR E 398  THR E 432                    
SITE     2 BC2 24 SER E 433  GLU E 434  ARG E 460  TYR E 463                    
SITE     3 BC2 24 PRO E 490  PHE E 491  ASN E 492  ARG E 510                    
SITE     4 BC2 24 ALA E 511  GLN E 514  LYS E 526  LEU E 527                    
SITE     5 BC2 24 ILE E 528  GLN E 533  ARG E 535  ILE E 574                    
SITE     6 BC2 24 TYR E 609  TYR E 613  ASP E 615  ARG E 619                    
SITE     1 BC3 24 ALA F 393  PRO F 395  TYR F 398  THR F 432                    
SITE     2 BC3 24 SER F 433  GLU F 434  ARG F 460  TYR F 463                    
SITE     3 BC3 24 PRO F 490  PHE F 491  ASN F 492  ARG F 510                    
SITE     4 BC3 24 ALA F 511  GLN F 514  LYS F 526  LEU F 527                    
SITE     5 BC3 24 ILE F 528  GLN F 533  ARG F 535  ILE F 574                    
SITE     6 BC3 24 TYR F 609  TYR F 613  ASP F 615  ARG F 619                    
CRYST1  151.689  166.227  261.992  90.00  90.00  90.00 P 21 21 21   24          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.006592  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006016  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003817        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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